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Conserved domains on  [gi|226693354|ref|NP_003697|]
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cytosolic phospholipase A2 gamma isoform 1 precursor [Homo sapiens]

Protein Classification

patatin-like phospholipase domain-containing protein( domain architecture ID 10163301)

patatin-like phospholipase domain-containing protein may function as a lipid acyl hydrolase, catalyzing the cleavage of fatty acids from membrane lipids

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
cPLA2_Grp-IVC cd07202
Group IVC cytoplasmic phospholipase A2; catalytic domain; Ca-independent; Group IVC cPLA2, a ...
4-529 0e+00

Group IVC cytoplasmic phospholipase A2; catalytic domain; Ca-independent; Group IVC cPLA2, a small 61 kDa protein, is a single domain alpha/beta hydrolase. It lacks a C2 domain; therefore, it has no Ca-dependence. Group IVC cPLA2 is also referred to as cPLA2-gamma. The cPLA2-gamma enzyme is predominantly found in cardiac and skeletal muscles, and to a lesser extent in the brain. Human cPLA2-gamma is approximately 30% identical to cPLA2-alpha. The catalytic domain of cytosolic phospholipase A2 (PLA2; EC 3.1.1.4) hydrolyzes the sn-2-acyl ester bond of phospholipids to release arachidonic acid. At the active site, cPLA2 contains a serine nucleophile through which the catalytic mechanism is initiated. The active site is partially covered by a solvent-accessible flexible lid. cPLA2 displays interfacial activation as it exists in both "closed lid" and "open lid" forms. Movement of the cPLA2 lid possibly exposes a greater hydrophobic surface and the active site. cPLA2 belongs to the alpha-beta hydrolase family which is identified by a characteristic nucleophile elbow with a consensus sequence of Sm-X-Nu-Sm (Sm = small residue, X = any residue and Nu = nucleophile). Includes PLA2G4C protein from human and Pla2g4c protein from mouse.


:

Pssm-ID: 132841 [Multi-domain]  Cd Length: 430  Bit Score: 726.58  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693354   4 SEVSIIPGLQKEEKAAVERRRLHVLKALKKLRIEADEAPVVAVLGSGGGLRAHIACLGVLSEMKEQGLLDAVTYLAGVSG 83
Cdd:cd07202    1 SEVRIAPGLNKEEKAAVVKRRKDVLQSLQKLGINADKAPVIAVLGSGGGLRAMIACLGVLSELDKAGLLDCVTYLAGVSG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693354  84 STWAISSLYTNDG---DMEALEADLKHRFTRQEWDLAKSLQKTIQAARSENYSLTDFWAYMVISKQTRELPESHLSNMKK 160
Cdd:cd07202   81 STWCMSSLYTEPDwstKLQTVEDELKRRLQKVSWDFAYALKKEIQAAKSDNFSLTDFWAYLVVTTFTKELDESTLSDQRK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693354 161 PVEEGTLPYPIFAAIDNDLqPSWQEARAPETWFEFTPHHAGFSALGAFVSITHFGSKFKKGRLVRTHPERDLTFLRGLWG 240
Cdd:cd07202  161 QSEEGKDPYPIFAAIDKDL-SEWKERKTGDPWFEFTPHEAGYPLPGAFVSTTHFGSKFENGKLVKQEPERDLLYLRALWG 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693354 241 SALGNTEVIREYifdqlrnltlkglwrravanaksighlifarllrlqessqgehpppedeggepehtwltemlenwtrt 320
Cdd:cd07202  240 SALADGEEIAKY-------------------------------------------------------------------- 251
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693354 321 slekqeqphedperkgslsnlmdfvkktgICASKWEWGTTHNFLYKHGGIRDKI-MSSRKHLHLVDAGLAINTPFPLVLP 399
Cdd:cd07202  252 -----------------------------ICMSLWIWGTTYNFLYKHGDIADKPaMRSRETLHLMDAGLAINSPYPLVLP 302
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693354 400 PTREVHLILSFDFSAGDPFETIRATTDYCRRHKIPFPQVEEAELDLWSKAPASCYILKGETGPVVMHFPLFNIDACGGDI 479
Cdd:cd07202  303 PVRNTDLILSFDFSEGDPFETIKDTAEYCRKHNIPFPQVDEAKLDQDAEAPKDFYVFKGENGPVVMHFPLFNKVNCGDQL 382
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|
gi 226693354 480 EAWSDTYDTFKlaDTYTLDVVVLLLALAKKNVRENKKKILRELMNVAGLY 529
Cdd:cd07202  383 EDWRKEYRTFQ--GAYSTDQVRQLLELAKANVKNNKEKIMSEIRALAGQI 430
 
Name Accession Description Interval E-value
cPLA2_Grp-IVC cd07202
Group IVC cytoplasmic phospholipase A2; catalytic domain; Ca-independent; Group IVC cPLA2, a ...
4-529 0e+00

Group IVC cytoplasmic phospholipase A2; catalytic domain; Ca-independent; Group IVC cPLA2, a small 61 kDa protein, is a single domain alpha/beta hydrolase. It lacks a C2 domain; therefore, it has no Ca-dependence. Group IVC cPLA2 is also referred to as cPLA2-gamma. The cPLA2-gamma enzyme is predominantly found in cardiac and skeletal muscles, and to a lesser extent in the brain. Human cPLA2-gamma is approximately 30% identical to cPLA2-alpha. The catalytic domain of cytosolic phospholipase A2 (PLA2; EC 3.1.1.4) hydrolyzes the sn-2-acyl ester bond of phospholipids to release arachidonic acid. At the active site, cPLA2 contains a serine nucleophile through which the catalytic mechanism is initiated. The active site is partially covered by a solvent-accessible flexible lid. cPLA2 displays interfacial activation as it exists in both "closed lid" and "open lid" forms. Movement of the cPLA2 lid possibly exposes a greater hydrophobic surface and the active site. cPLA2 belongs to the alpha-beta hydrolase family which is identified by a characteristic nucleophile elbow with a consensus sequence of Sm-X-Nu-Sm (Sm = small residue, X = any residue and Nu = nucleophile). Includes PLA2G4C protein from human and Pla2g4c protein from mouse.


Pssm-ID: 132841 [Multi-domain]  Cd Length: 430  Bit Score: 726.58  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693354   4 SEVSIIPGLQKEEKAAVERRRLHVLKALKKLRIEADEAPVVAVLGSGGGLRAHIACLGVLSEMKEQGLLDAVTYLAGVSG 83
Cdd:cd07202    1 SEVRIAPGLNKEEKAAVVKRRKDVLQSLQKLGINADKAPVIAVLGSGGGLRAMIACLGVLSELDKAGLLDCVTYLAGVSG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693354  84 STWAISSLYTNDG---DMEALEADLKHRFTRQEWDLAKSLQKTIQAARSENYSLTDFWAYMVISKQTRELPESHLSNMKK 160
Cdd:cd07202   81 STWCMSSLYTEPDwstKLQTVEDELKRRLQKVSWDFAYALKKEIQAAKSDNFSLTDFWAYLVVTTFTKELDESTLSDQRK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693354 161 PVEEGTLPYPIFAAIDNDLqPSWQEARAPETWFEFTPHHAGFSALGAFVSITHFGSKFKKGRLVRTHPERDLTFLRGLWG 240
Cdd:cd07202  161 QSEEGKDPYPIFAAIDKDL-SEWKERKTGDPWFEFTPHEAGYPLPGAFVSTTHFGSKFENGKLVKQEPERDLLYLRALWG 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693354 241 SALGNTEVIREYifdqlrnltlkglwrravanaksighlifarllrlqessqgehpppedeggepehtwltemlenwtrt 320
Cdd:cd07202  240 SALADGEEIAKY-------------------------------------------------------------------- 251
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693354 321 slekqeqphedperkgslsnlmdfvkktgICASKWEWGTTHNFLYKHGGIRDKI-MSSRKHLHLVDAGLAINTPFPLVLP 399
Cdd:cd07202  252 -----------------------------ICMSLWIWGTTYNFLYKHGDIADKPaMRSRETLHLMDAGLAINSPYPLVLP 302
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693354 400 PTREVHLILSFDFSAGDPFETIRATTDYCRRHKIPFPQVEEAELDLWSKAPASCYILKGETGPVVMHFPLFNIDACGGDI 479
Cdd:cd07202  303 PVRNTDLILSFDFSEGDPFETIKDTAEYCRKHNIPFPQVDEAKLDQDAEAPKDFYVFKGENGPVVMHFPLFNKVNCGDQL 382
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|
gi 226693354 480 EAWSDTYDTFKlaDTYTLDVVVLLLALAKKNVRENKKKILRELMNVAGLY 529
Cdd:cd07202  383 EDWRKEYRTFQ--GAYSTDQVRQLLELAKANVKNNKEKIMSEIRALAGQI 430
PLAc smart00022
Cytoplasmic phospholipase A2, catalytic subunit; Cytosolic phospholipases A2 hydrolyse ...
11-444 3.46e-35

Cytoplasmic phospholipase A2, catalytic subunit; Cytosolic phospholipases A2 hydrolyse arachidonyl phospholipids. Family includes phospholipases B isoforms.


Pssm-ID: 214474  Cd Length: 549  Bit Score: 138.71  E-value: 3.46e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693354    11 GLQKEEKAAVERRRLHVLKALKKL------------RIEADEAPVVAVLGSGGGLRAHIACLGVLSEMKEQ-------GL 71
Cdd:smart00022  33 GLSDNETEFLQKRKDYTNEAMKSFlgransnfldssLLNSSDVPKIAIAGSGGGFRAMVGGAGVLKAMDNRtdghglgGL 112
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693354    72 LDAVTYLAGVSGSTWAISSLYTN-----DGDMEA-LEADLKHR---------FTRQEWdlaKSLQKTIQAARSE--NYSL 134
Cdd:smart00022 113 LQSATYLAGLSGGTWLVGTLASNnftpvKGPEEInSEWMFSVSinnpginllLTAQFY---KSIVDAVWKKKDAgfNISL 189
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693354   135 TDFWAyMVISKQTRELPESH---LSNMK--KPVEEGTLPYPIFAAidNDLQPSWQEARAPETWFEFTPHHAG-FSA-LGA 207
Cdd:smart00022 190 TDIWG-RALSYNLFDSLGGPnytLSSLRdqEKFQNAEMPLPIFVA--DGRKPGESVINFNDTVFEFSPFEFGsWDPkLNA 266
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693354   208 FVSITHFGSKFKKGRLVRTHPERDLTFLRGLWGSAlgntevireyiFDQLRNLTLkGLWRRAVANAKSIGHLIFARLLRL 287
Cdd:smart00022 267 FMPPEYLGSKFFNGTPVKKGKCIPNFDNAGFIMGT-----------SSSLFNRFL-LVLSNSTMEESLIKIIIKHILKDL 334
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693354   288 QESSQGE--HPPpedeGGEPEHTWLTEMLEN--------WTRTSLEKQE--------QPHEDPERKGSLSNLMDfvkktg 349
Cdd:smart00022 335 SSDSDDIaiYPP----NPFKDDAYVQRMLTNslgdsdllNLVDGGEDGEniplspllQPERSVDVIFAVDASAD------ 404
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693354   350 icaSKWEWgtthnflykhgGIRDKIMSSRKhLHLVDAGLAINTPFPLVLPPTREVHLILSFDFSAGD----------PFE 419
Cdd:smart00022 405 ---TDEFW-----------PNGSSLVKTYE-RHVVDQGLTFNLPFPYVPDTQTFVNLGLSTKPTFFGcdssnltyipPLV 469
                          490       500
                   ....*....|....*....|....*
gi 226693354   420 TIRATTDYCRRHKIPFPQVEEAELD 444
Cdd:smart00022 470 VYLPNEKWAYNSNISTFKISYSVFE 494
PLA2_B pfam01735
Lysophospholipase catalytic domain; This family consists of Lysophospholipase / phospholipase ...
44-242 3.48e-24

Lysophospholipase catalytic domain; This family consists of Lysophospholipase / phospholipase B EC:3.1.1.5 and cytosolic phospholipase A2 EC:3.1.4 which also has a C2 domain pfam00168. Phospholipase B enzymes catalyze the release of fatty acids from lysophsopholipids and are capable in vitro of hydrolysing all phospholipids extractable form yeast cells. Cytosolic phospholipase A2 associates with natural membranes in response to physiological increases in Ca2+ and selectively hydrolyses arachidonyl phospholipids, the aligned region corresponds the the carboxy-terminal Ca2+-independent catalytic domain of the protein as discussed in.


Pssm-ID: 366778  Cd Length: 490  Bit Score: 105.92  E-value: 3.48e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693354   44 VAVLGSGGGLRAHIACLGVLSEM--------KEQGLLDAVTYLAGVSGSTWAISSLYTN-------------DGDMEALE 102
Cdd:pfam01735   1 IGIAGSGGGYRAMLGGAGVLAALdnrtdnetGLGGLLQSATYLAGLSGGSWLVGSLAVNnftsvqdfpdkpeDISIWDLN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693354  103 ------ADLKHRFTRQEWD-LAKSLQKtiQAARSENYSLTDFWAyMVISKQ----TRELPESHLSNMKKP--VEEGTLPY 169
Cdd:pfam01735  81 hsifnpGGLNIPQNIKRYDdIVDAVWK--KKNAGFNVSLTDIWG-RALSYTlipsLRGGPNYTWSSLRDAewFQNAEMPF 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 226693354  170 PIFAAiDNdLQPSWQEARAPETWFEFTPHHAGF--SALGAFVSITHFGSKFKKGRLVRTHPERDLTFLRGLWGSA 242
Cdd:pfam01735 158 PIIVA-DG-RKPGTTVINLNATVFEFSPYEFGSwdPTLNSFTPTEYLGTKFFNGTPVKKGKCVPGFDNAGFVMGT 230
 
Name Accession Description Interval E-value
cPLA2_Grp-IVC cd07202
Group IVC cytoplasmic phospholipase A2; catalytic domain; Ca-independent; Group IVC cPLA2, a ...
4-529 0e+00

Group IVC cytoplasmic phospholipase A2; catalytic domain; Ca-independent; Group IVC cPLA2, a small 61 kDa protein, is a single domain alpha/beta hydrolase. It lacks a C2 domain; therefore, it has no Ca-dependence. Group IVC cPLA2 is also referred to as cPLA2-gamma. The cPLA2-gamma enzyme is predominantly found in cardiac and skeletal muscles, and to a lesser extent in the brain. Human cPLA2-gamma is approximately 30% identical to cPLA2-alpha. The catalytic domain of cytosolic phospholipase A2 (PLA2; EC 3.1.1.4) hydrolyzes the sn-2-acyl ester bond of phospholipids to release arachidonic acid. At the active site, cPLA2 contains a serine nucleophile through which the catalytic mechanism is initiated. The active site is partially covered by a solvent-accessible flexible lid. cPLA2 displays interfacial activation as it exists in both "closed lid" and "open lid" forms. Movement of the cPLA2 lid possibly exposes a greater hydrophobic surface and the active site. cPLA2 belongs to the alpha-beta hydrolase family which is identified by a characteristic nucleophile elbow with a consensus sequence of Sm-X-Nu-Sm (Sm = small residue, X = any residue and Nu = nucleophile). Includes PLA2G4C protein from human and Pla2g4c protein from mouse.


Pssm-ID: 132841 [Multi-domain]  Cd Length: 430  Bit Score: 726.58  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693354   4 SEVSIIPGLQKEEKAAVERRRLHVLKALKKLRIEADEAPVVAVLGSGGGLRAHIACLGVLSEMKEQGLLDAVTYLAGVSG 83
Cdd:cd07202    1 SEVRIAPGLNKEEKAAVVKRRKDVLQSLQKLGINADKAPVIAVLGSGGGLRAMIACLGVLSELDKAGLLDCVTYLAGVSG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693354  84 STWAISSLYTNDG---DMEALEADLKHRFTRQEWDLAKSLQKTIQAARSENYSLTDFWAYMVISKQTRELPESHLSNMKK 160
Cdd:cd07202   81 STWCMSSLYTEPDwstKLQTVEDELKRRLQKVSWDFAYALKKEIQAAKSDNFSLTDFWAYLVVTTFTKELDESTLSDQRK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693354 161 PVEEGTLPYPIFAAIDNDLqPSWQEARAPETWFEFTPHHAGFSALGAFVSITHFGSKFKKGRLVRTHPERDLTFLRGLWG 240
Cdd:cd07202  161 QSEEGKDPYPIFAAIDKDL-SEWKERKTGDPWFEFTPHEAGYPLPGAFVSTTHFGSKFENGKLVKQEPERDLLYLRALWG 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693354 241 SALGNTEVIREYifdqlrnltlkglwrravanaksighlifarllrlqessqgehpppedeggepehtwltemlenwtrt 320
Cdd:cd07202  240 SALADGEEIAKY-------------------------------------------------------------------- 251
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693354 321 slekqeqphedperkgslsnlmdfvkktgICASKWEWGTTHNFLYKHGGIRDKI-MSSRKHLHLVDAGLAINTPFPLVLP 399
Cdd:cd07202  252 -----------------------------ICMSLWIWGTTYNFLYKHGDIADKPaMRSRETLHLMDAGLAINSPYPLVLP 302
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693354 400 PTREVHLILSFDFSAGDPFETIRATTDYCRRHKIPFPQVEEAELDLWSKAPASCYILKGETGPVVMHFPLFNIDACGGDI 479
Cdd:cd07202  303 PVRNTDLILSFDFSEGDPFETIKDTAEYCRKHNIPFPQVDEAKLDQDAEAPKDFYVFKGENGPVVMHFPLFNKVNCGDQL 382
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|
gi 226693354 480 EAWSDTYDTFKlaDTYTLDVVVLLLALAKKNVRENKKKILRELMNVAGLY 529
Cdd:cd07202  383 EDWRKEYRTFQ--GAYSTDQVRQLLELAKANVKNNKEKIMSEIRALAGQI 430
cPLA2_like cd00147
Cytosolic phospholipase A2, catalytic domain; hydrolyses arachidonyl phospholipids; Catalytic ...
6-524 1.33e-146

Cytosolic phospholipase A2, catalytic domain; hydrolyses arachidonyl phospholipids; Catalytic domain of cytosolic phospholipase A2 (PLA2; EC 3.1.1.4) hydrolyzes the sn-2-acyl ester bond of phospholipids to release arachidonic acid. At the active site, cPLA2 contains a serine nucleophile through which the catalytic mechanism is initiated. The active site is partially covered by a solvent-accessible flexible lid. cPLA2 displays interfacial activation as it exists in both "closed lid" and "open lid" forms. Movement of the cPLA2 lid possibly exposes a greater hydrophobic surface and the active site. cPLA2 belongs to the alpha-beta hydrolase family which is identified by a characteristic nucleophile elbow with a consensus sequence of Sm-X-Nu-Sm (Sm = small residue, X = any residue and Nu = nucleophile). Calcium is required for cPLA2 to bind with membranes or phospholipids. Group IV cPLA2 includes six intercellular enzymes: cPLA2alpha, cPLA2beta, cPLA2gamma, cPLA2delta, cPLA2epsilon, and cPLA2zeta.


Pssm-ID: 132835 [Multi-domain]  Cd Length: 438  Bit Score: 428.59  E-value: 1.33e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693354   6 VSIIPGLQKEEKAAVERRRLHVLKALKKLRIEA-----DEAPVVAVLGSGGGLRAHIACLGVLSEMKEQGLLDAVTYLAG 80
Cdd:cd00147    1 VRLASDLCDEEKEFLEKRRKVVAKALKKFLGLEndlnpDEVPVIAILGSGGGYRAMTGGAGALKALDEGGLLDCVTYLSG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693354  81 VSGSTWAISSLYTNDG----DMEALEADLKHR---------FTRQEWDLAKSLQKTIQAArsENYSLTDFWAYMVISKQT 147
Cdd:cd00147   81 LSGSTWLMASLYSNPDwsqkDLDEAIEWLKRHviksplllfSPERLKYYAKELEEKKKAG--FNVSLTDFWGLLLGYTLL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693354 148 RELPESHLSNMKKPVEEGTLPYPIFAAIDNDLQPswQEARAPETWFEFTPHHAGFSALGAFVSITHFGSKFKKGRLVRTH 227
Cdd:cd00147  159 KELTDSSLSDQREFVQNGQNPLPIYTALNVKPGE--TSINDFATWFEFTPYEVGFPKYGAFIPTEYFGSKFFMGRLVKKI 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693354 228 PERDLTFLRGLWGSALGNtevireyifdqlrnltlkglwrravanaksighlifarllrlqessqgehpppedeggepeh 307
Cdd:cd00147  237 PEDRLGFLMGTWGSAFSI-------------------------------------------------------------- 254
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693354 308 twltemlenwtrtslekqeqphedperkgslsNLMDfvkktgicaskweWGTTHNFLYKHGGIRD------KIMSSRKHL 381
Cdd:cd00147  255 --------------------------------ILLD-------------AGKYPNFFYGLNLHKSylrspnPLITSSDTL 289
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693354 382 HLVDAGLAINT-PFPLVLPPTREVHLILSFDFSAGDP--FETIRATTDYCRRH---KIPFPQVEEAELdLWSKAPASCYI 455
Cdd:cd00147  290 HLVDAGLDINNiPLPPLLRPERDVDVILSFDFSADDPdwPNGLKLVATYERQAssnGIPFPKIPDSVT-FDNLGLKECYV 368
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 226693354 456 LKGE---TGPVVMHFPLFNIDACGGDIEAWSDTYDTFKLadTYTLDVVVLLLALAKKNVRENKKKILRELMN 524
Cdd:cd00147  369 FFGCddpDAPLVVYFPLVNDTFRKYDFDDPNSPYSTFNL--SYTDEEFDRLLELAFYNVTNNKDTILQALRA 438
cPLA2_Grp-IVB-IVD-IVE-IVF cd07201
Group IVB, IVD, IVE, and IVF cytosolic phospholipase A2; catalytic domain; Ca-dependent; Group ...
11-471 1.34e-73

Group IVB, IVD, IVE, and IVF cytosolic phospholipase A2; catalytic domain; Ca-dependent; Group IVB, IVD, IVE, and IVF cPLA2 consists of two domains: the regulatory C2 domain and alpha/beta hydrolase PLA2 domain. Group IVB, IVD, IVE, and IVF cPLA2 are also referred to as cPLA2-beta, -delta, -epsilon, and -zeta respectively. cPLA2-beta is approximately 30% identical to cPLA2-alpha and it shows low enzymatic activity compared to cPLA2alpha. cPLA2-beta hydrolyzes palmitic acid from 1-[14C]palmitoyl-2-arachidonoyl-PC and arachidonic acid from 1-palmitoyl-2[14C]arachidonoyl-PC, but not from 1-O-alkyl-2[3H]arachidonoyl-PC. cPLA2-delta, -epsilon, and -zeta are approximately 45-50% identical to cPLA2-beta and 31-37% identical to cPLA2-alpha. It's possible that cPLA2-beta, -delta, -epsilon, and -zeta may have arisen by gene duplication from an ancestral gene. The catalytic domain of cytosolic phospholipase A2 (PLA2; EC 3.1.1.4) hydrolyzes the sn-2-acyl ester bond of phospholipids to release arachidonic acid. At the active site, cPLA2 contains a serine nucleophile through which the catalytic mechanism is initiated. The active site is partially covered by a solvent-accessible flexible lid. cPLA2 displays interfacial activation as it exists in both "closed lid" and "open lid" forms. Movement of the cPLA2 lid possibly exposes a greater hydrophobic surface and the active site. cPLA2 belongs to the alpha-beta hydrolase family which is identified by a characteristic nucleophile elbow with a consensus sequence of Sm-X-Nu-Sm (Sm = small residue, X = any residue and Nu = nucleophile). Calcium is required for cPLA2 to bind with membranes or phospholipids. The calcium-dependent phospholipid binding domain resides in the N-terminal region of cPLA2; it is homologous to the C2 domain superfamily which is not included in this hierarchy. It includes PLA2G4B, PLA2G4D, PLA2G4E, and PLA2G4F from humans.


Pssm-ID: 132840 [Multi-domain]  Cd Length: 541  Bit Score: 243.40  E-value: 1.34e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693354  11 GLQKEEKAAVERRRLHVLKALKK-LRIEAD----EAPVVAVLGSGGGLRAHIACLGVLSEMKEQGLLDAVTYLAGVSGST 85
Cdd:cd07201   17 DLCAEEQEFLQKRKKVVAAALKKaLQLEEDlqedEVPVVAVMTTGGGTRALTSMYGSLLGLQKLGLLDCVSYITGLSGST 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693354  86 WAISSLYtndGDMEALEADLKHRFTRQEWDLAKS---------LQKTIQ--AARSE---NYSLTDFWAYMVISKQTRELP 151
Cdd:cd07201   97 WTMATLY---EDPNWSQKDLEGPIEEARKHVTKSklgcfsperLKYYRQelSEREQeghKVSFIDLWGLIIESMLHDKKN 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693354 152 ESHLSNMKKPVEEGTLPYPIFAAIDNDLQPSWQEARapeTWFEFTPHHAGFSALGAFVSITHFGSKFKKGRLVRTHPERD 231
Cdd:cd07201  174 DHKLSDQREAVSQGQNPLPIYLSLNVKDNLSTQDFR---EWVEFTPYEVGFLKYGAFIPAEDFGSEFFMGRLMKKLPESR 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693354 232 LTFLRGLWGSalgntevireyIFdqlrNLTLKGLWRRAVanaksighlifarllrlqessqgehpppedeggEPEHTWLt 311
Cdd:cd07201  251 ICFLQGMWSS-----------IF----SLNLLDAWYLAT---------------------------------GSEDFWH- 281
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693354 312 emleNWTR---TSLEKQEQPHEDPER--------KGSLSN-LMDFVKKTGICASkwewgtTHNFL---------YKHGGI 370
Cdd:cd07201  282 ----RWTRdkvNDIEDEPPLPPRPPErlttlltpGGPLSQaFRDFLTSRPTVSQ------YFNFLrglqlhndyLENKGF 351
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693354 371 ---RDKIM--------SSRKHLHLVDAGLAINTPFPLVLPPTREVHLILSFDFSAGDPFETIRATTDYCRRHKIPFPQVE 439
Cdd:cd07201  352 stwKDTHLdafpnqltPSEDHLCLVDTAFFINTSYPPLLRPERKVDVILSLNYSLGSQFEPLKQASEYCSEQGIPFPKIE 431
                        490       500       510
                 ....*....|....*....|....*....|....*
gi 226693354 440 EAELDlwSKAPASCYILKGET---GPVVMHFPLFN 471
Cdd:cd07201  432 LSPED--QENLKECYVFEDADnpeAPIVLHFPLVN 464
cPLA2_Grp-IVA cd07200
Group IVA cytosolic phospholipase A2; catalytic domain; Ca-dependent; Group IVA cPLA2, an 85 ...
12-472 1.88e-60

Group IVA cytosolic phospholipase A2; catalytic domain; Ca-dependent; Group IVA cPLA2, an 85 kDa protein, consists of two domains: the regulatory C2 domain and the alpha/beta hydrolase PLA2 domain. Group IVA cPLA2 is also referred to as cPLA2-alpha. The catalytic domain of cytosolic phospholipase A2 (cPLA2; EC 3.1.1.4) hydrolyzes the sn-2-acyl ester bond of phospholipids to release arachidonic acid. At the active site, cPLA2 contains a serine nucleophile through which the catalytic mechanism is initiated. The active site is partially covered by a solvent-accessible flexible lid. cPLA2 displays interfacial activation as it exists in both "closed lid" and "open lid" forms. Movement of the cPLA2 lid possibly exposes a greater hydrophobic surface and the active site. cPLA2 belongs to the alpha-beta hydrolase family which is identified by a characteristic nucleophile elbow with a consensus sequence of Sm-X-Nu-Sm (Sm = small residue, X = any residue and Nu = nucleophile). Calcium is required for cPLA2 to bind with membranes or phospholipids. A calcium-dependent phospholipid binding domain resides in the N-terminal region of cPLA2; it is homologous to the C2 domain superfamily which is not included in this hierarchy. Includes PLA2G4A from chicken, human, and frog.


Pssm-ID: 132839  Cd Length: 505  Bit Score: 207.69  E-value: 1.88e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693354  12 LQKEEKAAVERRRLHVLKALKKL-------RIEADEAPVVAVLGSGGGLRAHIACLGVLSEMKEQGLLDAVTYLAGVSGS 84
Cdd:cd07200    7 LCDEEKEFRQARKMRVREALRKLlgeegpkVTSLREVPVIALLGSGGGFRAMVGMSGAMKALYDSGVLDCATYVAGLSGS 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693354  85 TWAISSLYTNdGDMEALEADLKHRFTRQewDLAKSLQKTIQAARSENY--------------SLTDFWAYMVISKQTREL 150
Cdd:cd07200   87 TWYMSTLYSH-PDFPEKGPGEINKELMR--NVSSSPLLLLTPQLLKRYtealwekkssgqpvTFTDFFGMLIGETLIKER 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693354 151 PESHLSNMKKPVEEGTLPYPIFAA--IDNDLQPSWQEArapetWFEFTPHHAGFSALGAFVSITHFGSKFKKGRLVRTHP 228
Cdd:cd07200  164 MDTKLSDLQEKVNDGQVPLPLFTClhVKPDVSALMFHD-----WVEFSPYEIGMAKYGTFMSPDLFGSKFFMGFLAKKYP 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693354 229 ERDLTFLRGLWGSALGntevireYIFDQLRNLTLKgLWRRA-VANaksighliFARLLRLQEssqgehpppedeggepeh 307
Cdd:cd07200  239 ENPLHFLMGVWGSAFS-------ILFNRVLGRNSR-EGRAGkVHN--------FMLGLNLNT------------------ 284
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693354 308 twlTEMLENWTRTSLEKQEQPHEDPERKGSlsnlmdfvkktgicaskwewgtthnflykhggIRDKIMSSRKHLHLVDAG 387
Cdd:cd07200  285 ---SYPLSPLSDLATDEPEAAVADADEFER--------------------------------IYEPLDTKSKKIHVVDSG 329
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693354 388 LAINTPFPLVLPPTREVHLILSFDFSAGD-----PFETIRATTDYCRRHKIPFPQVEEAELDlwSKAPASCYILKGETG- 461
Cdd:cd07200  330 LTFNLPYPLILRPQRGVDLIISFDFSARPsdsspPFKELLLAEKWARMNGLPFPPIDFKVFD--REGLKECYVFKPKNDd 407
                        490
                 ....*....|...
gi 226693354 462 --PVVMHFPLFNI 472
Cdd:cd07200  408 dcPTVIHFVLCNI 420
PLAc smart00022
Cytoplasmic phospholipase A2, catalytic subunit; Cytosolic phospholipases A2 hydrolyse ...
11-444 3.46e-35

Cytoplasmic phospholipase A2, catalytic subunit; Cytosolic phospholipases A2 hydrolyse arachidonyl phospholipids. Family includes phospholipases B isoforms.


Pssm-ID: 214474  Cd Length: 549  Bit Score: 138.71  E-value: 3.46e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693354    11 GLQKEEKAAVERRRLHVLKALKKL------------RIEADEAPVVAVLGSGGGLRAHIACLGVLSEMKEQ-------GL 71
Cdd:smart00022  33 GLSDNETEFLQKRKDYTNEAMKSFlgransnfldssLLNSSDVPKIAIAGSGGGFRAMVGGAGVLKAMDNRtdghglgGL 112
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693354    72 LDAVTYLAGVSGSTWAISSLYTN-----DGDMEA-LEADLKHR---------FTRQEWdlaKSLQKTIQAARSE--NYSL 134
Cdd:smart00022 113 LQSATYLAGLSGGTWLVGTLASNnftpvKGPEEInSEWMFSVSinnpginllLTAQFY---KSIVDAVWKKKDAgfNISL 189
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693354   135 TDFWAyMVISKQTRELPESH---LSNMK--KPVEEGTLPYPIFAAidNDLQPSWQEARAPETWFEFTPHHAG-FSA-LGA 207
Cdd:smart00022 190 TDIWG-RALSYNLFDSLGGPnytLSSLRdqEKFQNAEMPLPIFVA--DGRKPGESVINFNDTVFEFSPFEFGsWDPkLNA 266
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693354   208 FVSITHFGSKFKKGRLVRTHPERDLTFLRGLWGSAlgntevireyiFDQLRNLTLkGLWRRAVANAKSIGHLIFARLLRL 287
Cdd:smart00022 267 FMPPEYLGSKFFNGTPVKKGKCIPNFDNAGFIMGT-----------SSSLFNRFL-LVLSNSTMEESLIKIIIKHILKDL 334
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693354   288 QESSQGE--HPPpedeGGEPEHTWLTEMLEN--------WTRTSLEKQE--------QPHEDPERKGSLSNLMDfvkktg 349
Cdd:smart00022 335 SSDSDDIaiYPP----NPFKDDAYVQRMLTNslgdsdllNLVDGGEDGEniplspllQPERSVDVIFAVDASAD------ 404
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693354   350 icaSKWEWgtthnflykhgGIRDKIMSSRKhLHLVDAGLAINTPFPLVLPPTREVHLILSFDFSAGD----------PFE 419
Cdd:smart00022 405 ---TDEFW-----------PNGSSLVKTYE-RHVVDQGLTFNLPFPYVPDTQTFVNLGLSTKPTFFGcdssnltyipPLV 469
                          490       500
                   ....*....|....*....|....*
gi 226693354   420 TIRATTDYCRRHKIPFPQVEEAELD 444
Cdd:smart00022 470 VYLPNEKWAYNSNISTFKISYSVFE 494
PLA2_B pfam01735
Lysophospholipase catalytic domain; This family consists of Lysophospholipase / phospholipase ...
44-242 3.48e-24

Lysophospholipase catalytic domain; This family consists of Lysophospholipase / phospholipase B EC:3.1.1.5 and cytosolic phospholipase A2 EC:3.1.4 which also has a C2 domain pfam00168. Phospholipase B enzymes catalyze the release of fatty acids from lysophsopholipids and are capable in vitro of hydrolysing all phospholipids extractable form yeast cells. Cytosolic phospholipase A2 associates with natural membranes in response to physiological increases in Ca2+ and selectively hydrolyses arachidonyl phospholipids, the aligned region corresponds the the carboxy-terminal Ca2+-independent catalytic domain of the protein as discussed in.


Pssm-ID: 366778  Cd Length: 490  Bit Score: 105.92  E-value: 3.48e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693354   44 VAVLGSGGGLRAHIACLGVLSEM--------KEQGLLDAVTYLAGVSGSTWAISSLYTN-------------DGDMEALE 102
Cdd:pfam01735   1 IGIAGSGGGYRAMLGGAGVLAALdnrtdnetGLGGLLQSATYLAGLSGGSWLVGSLAVNnftsvqdfpdkpeDISIWDLN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693354  103 ------ADLKHRFTRQEWD-LAKSLQKtiQAARSENYSLTDFWAyMVISKQ----TRELPESHLSNMKKP--VEEGTLPY 169
Cdd:pfam01735  81 hsifnpGGLNIPQNIKRYDdIVDAVWK--KKNAGFNVSLTDIWG-RALSYTlipsLRGGPNYTWSSLRDAewFQNAEMPF 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 226693354  170 PIFAAiDNdLQPSWQEARAPETWFEFTPHHAGF--SALGAFVSITHFGSKFKKGRLVRTHPERDLTFLRGLWGSA 242
Cdd:pfam01735 158 PIIVA-DG-RKPGTTVINLNATVFEFSPYEFGSwdPTLNSFTPTEYLGTKFFNGTPVKKGKCVPGFDNAGFVMGT 230
Patatin_and_cPLA2 cd01819
Patatins and Phospholipases; Patatin-like phospholipase. This family consists of various ...
46-410 4.23e-24

Patatins and Phospholipases; Patatin-like phospholipase. This family consists of various patatin glycoproteins from plants. The patatin protein accounts for up to 40% of the total soluble protein in potato tubers. Patatin is a storage protein, but it also has the enzymatic activity of a lipid acyl hydrolase, catalyzing the cleavage of fatty acids from membrane lipids. Members of this family have also been found in vertebrates. This family also includes the catalytic domain of cytosolic phospholipase A2 (PLA2; EC 3.1.1.4) hydrolyzes the sn-2-acyl ester bond of phospholipids to release arachidonic acid. At the active site, cPLA2 contains a serine nucleophile through which the catalytic mechanism is initiated. The active site is partially covered by a solvent-accessible flexible lid. cPLA2 displays interfacial activation as it exists in both "closed lid" and "open lid" forms.


Pssm-ID: 132836 [Multi-domain]  Cd Length: 155  Bit Score: 98.64  E-value: 4.23e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693354  46 VLGSGGGLRAhIACLGVLSEMKEQGLLDAVTYLAGVSGSTWAISSLYtndgdmealeadlkhrftrqewdlakslqktiq 125
Cdd:cd01819    1 LSFSGGGFRG-MYHAGVLSALAERGLLDCVTYLAGTSGGAWVAATLY--------------------------------- 46
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693354 126 aarsenysltdfwaymviskqtrelpeshlsnmkkpveegtlpyPIFAAIDNDLQPSWQEARAPETWFEFTPHHAGFSAL 205
Cdd:cd01819   47 --------------------------------------------PPSSSLDNKPRQSLEEALSGKLWVSFTPVTAGENVL 82
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693354 206 GAfvsithfgskfkkgRLVRTHPERDLTFLRGLWGSALGNTEVIREYIfdqlrnltlkglwrravanaksighlifarll 285
Cdd:cd01819   83 VS--------------RFVSKEELIRALFASGSWPSYFGLIPPAELYT-------------------------------- 116
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693354 286 rlqessqgehpppedeggepehtwltemlenwtrtslekqeqphedperkgslsnlmdfvkktgicaskwewgtthnfly 365
Cdd:cd01819      --------------------------------------------------------------------------------
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 226693354 366 khggirDKIMSSRKHLHLVDAGLAINTPFPLVLPPTREVHLILSF 410
Cdd:cd01819  117 ------SKSNLKEKGVRLVDGGVSNNLPAPVLLRPGRGVTLTISP 155
cPLA2_Fungal_PLB cd07203
Fungal Phospholipase B-like; cPLA2 GrpIVA homologs; catalytic domain; Fungal phospholipase B ...
11-225 1.58e-15

Fungal Phospholipase B-like; cPLA2 GrpIVA homologs; catalytic domain; Fungal phospholipase B are Group IV cPLA2 homologs. Aspergillus PLA2 is Ca-dependent, yet it does not contain a C2 domain. PLB deacylates both sn-1 and sn-2 chains of phospholipids and are abundantly expressed in fungi. It shows lysophospholipase (lysoPL) and transacylase activities. The active site residues from cPLA2 are also conserved in PLB. Like cPLA2, PLB also has a consensus sequence of Sm-X-Nu-Sm (Sm = small residue, X = any residue and Nu = nucleophile). It includes PLB1 from Schizosaccharomyces pombe, PLB2 from Candida glabrata, and PLB3 from Saccharomyces cerevisiae. PLB1, PLB2, and PLB3 show PLB and lysoPL activities; PLB3 is specific for phosphoinositides.


Pssm-ID: 132842  Cd Length: 552  Bit Score: 79.33  E-value: 1.58e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693354  11 GLQKEEKAAVERRRLHVLKALK-------------KLRIEADEAPVVAVLGSGGGLRAHIACLGVLSEMKEQ-------- 69
Cdd:cd07203   19 GLSTNEQEYLEKRRSITNSALKdflsranlngdddLDSNNSSNGPRIGIAVSGGGYRAMLTGAGAIAAMDNRtdnatehg 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693354  70 --GLLDAVTYLAGVSGSTWAISSLYTN---------DGDMEALE------ADLKHRFTRQEWDlakSLQKTIQAARSENY 132
Cdd:cd07203   99 lgGLLQSSTYLSGLSGGSWLVGSLASNnftsvqdllADSIWNLDhsifnpYGAAIVKTLNYYT---NLANEVAQKKDAGF 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693354 133 --SLTDFW----AYMVISkQTRELPESHLSNMKKPVE--EGTLPYPIFAAidNDLQPSWQEARAPETWFEFTPHHAGF-- 202
Cdd:cd07203  176 nvSLTDIWgralSYQLFP-ALRGGPNLTWSSIRNQSWfqNAEMPFPIIVA--DGRYPGETIINLNATVFEFTPYEFGSwd 252
                        250       260
                 ....*....|....*....|...
gi 226693354 203 SALGAFVSITHFGSKFKKGRLVR 225
Cdd:cd07203  253 PSLNSFTPTEYLGTNVSNGVPPN 275
Pat_PNPLA6_PNPLA7_NTE1_like cd07205
Patatin-like phospholipase domain containing protein 6, protein 7, and fungal NTE1; ...
49-111 5.26e-03

Patatin-like phospholipase domain containing protein 6, protein 7, and fungal NTE1; Patatin-like phospholipase domain containing protein 6 (PNPLA6) and protein 7 (PNPLA7) are included in this family. PNPLA6 is commonly known as Neuropathy Target Esterase (NTE). NTE has at least two functional domains: the N-terminal domain putatively regulatory domain and the C-terminal catalytic domain which shows esterase activity. NTE shows phospholipase activity for lysophosphatidylcholine (LPC) and phosphatidylcholine (PC). Exposure of NTE to organophosphates leads to organophosphate-induced delayed neurotoxicity (OPIDN). OPIDN is a progressive neurological condition that is characterized by weakness, paralysis, pain, and paresthesia. PNPLA7 is an insulin-regulated phospholipase that is homologus to Neuropathy Target Esterase (NTE or PNPLA6) and is also known as NTE-related esterase (NRE). Human NRE is predominantly expressed in prostate, white adipose, and pancreatic tissue. NRE hydrolyzes sn-1 esters in lysophosphatidylcholine and lysophosphatidic acid, but shows no lipase activity with substrates like triacylglycerols (TG), cholesteryl esters, retinyl esters (RE), phosphatidylcholine (PC), or monoacylglycerol (MG). This family includes subfamily of PNPLA6 (NTE) and PNPLA7 (NRE)-like phospholipases.


Pssm-ID: 132844 [Multi-domain]  Cd Length: 175  Bit Score: 37.91  E-value: 5.26e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 226693354  49 SGGGLR--AHIaclGVLSEMKEQGLldAVTYLAGVS-GStwAISSLY---TNDGDMEALEADLKHRFTR 111
Cdd:cd07205    6 SGGGARglAHI---GVLKALEEAGI--PIDIVSGTSaGA--IVGALYaagYSPEEIEERAKLRSTDLKA 67
 
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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