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Conserved domains on  [gi|448520557|ref|XP_003868306|]
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hypothetical protein CORT_0C00230 [Candida orthopsilosis Co 90-125]

Protein Classification

patatin-like phospholipase domain-containing protein( domain architecture ID 27818)

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
Patatin_and_cPLA2 super family cl11396
Patatins and Phospholipases; Patatin-like phospholipase. This family consists of various ...
171-727 0e+00

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.


The actual alignment was detected with superfamily member cd07203:

Pssm-ID: 416256  Cd Length: 552  Bit Score: 618.61  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 448520557 171 PVNVTCPGDV-LVREG-DGLSDNEKNYIEAKQEQTNKFLISFLNnRANLSNFDAESFINDnsdEHNITIGLAFSGGGYRA 248
Cdd:cd07203    1 PFNVSCPSDAnLIRSAsDGLSTNEQEYLEKRRSITNSALKDFLS-RANLNGDDDLDSNNS---SNGPRIGIAVSGGGYRA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 448520557 249 MLAGAGSILALDNRFEDSNTNALGGLLQASTYLVGLSGGSWMVGTLVLNDWISVENILNGSsqIWDLEASILDPNAGDLI 328
Cdd:cd07203   77 MLTGAGAIAAMDNRTDNATEHGLGGLLQSSTYLSGLSGGSWLVGSLASNNFTSVQDLLADS--IWNLDHSIFNPYGAAIV 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 448520557 329 ELARFYTGVGTAIVNKNRAGFNTSATDIWGRALSHQFLDDSSGGANLTWSSIRNLTSFKDHSMPYTILIANGKTVEAEVI 408
Cdd:cd07203  155 KTLNYYTNLANEVAQKKDAGFNVSLTDIWGRALSYQLFPALRGGPNLTWSSIRNQSWFQNAEMPFPIIVADGRYPGETII 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 448520557 409 SPNSTFIvEISPYELGNRD-ALNAFVDTEYLGSSLEDGDSH--QCVKNFDNAGFVMGTSSSVFNSVFSNLDDYDVSTVLR 485
Cdd:cd07203  235 NLNATVF-EFTPYEFGSWDpSLNSFTPTEYLGTNVSNGVPPngSCVNGFDNAGFVMGTSSTLFNQFLLQINSTSSPSFIK 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 448520557 486 PIFDQIMSVVSDTKDDVAVYKPNPFYETSYAQVDT---IINNNTLLLVDGGENGQNVPFYPLIQSDRGVDVILAFDNSAD 562
Cdd:cd07203  314 LIATGFLLDILKENQDIASYIPNPFQGYTYSNSNGtnpIVDSDYLDLVDGGEDGQNIPLWPLLQPERDVDVIFAFDSSAD 393
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 448520557 563 TKENWPNGTSFTETYKWQFTNQGK-GTPFPYVPTVDTYLSEDLKEKPIFFGCNASALSDivdfhndNDLNETDVPLVVYL 641
Cdd:cd07203  394 TDYNWPNGTSLVATYERQFSSQGNnGTGFPYVPDQNTFVNLGLNDRPTFFGCDGRNLTD-------LNVDQYTPPLVVYI 466
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 448520557 642 SNHHESYLSNFSTFKLAYDNAEKTGTIRNGYEVMSRGNLTDDSNWATCVGCAIIRRQQERLGEEQSEECAKCFQEYCWTG 721
Cdd:cd07203  467 PNAPWSYNSNISTFKLSYTDSERQGMILNGFESATRNNLTNDDEFATCVACAIIRRSLERLNITTPDECQQCFDNYCWNG 546

                 ....*.
gi 448520557 722 TAKDAP 727
Cdd:cd07203  547 TIDTTP 552
 
Name Accession Description Interval E-value
cPLA2_Fungal_PLB cd07203
Fungal Phospholipase B-like; cPLA2 GrpIVA homologs; catalytic domain; Fungal phospholipase B ...
171-727 0e+00

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: 618.61  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 448520557 171 PVNVTCPGDV-LVREG-DGLSDNEKNYIEAKQEQTNKFLISFLNnRANLSNFDAESFINDnsdEHNITIGLAFSGGGYRA 248
Cdd:cd07203    1 PFNVSCPSDAnLIRSAsDGLSTNEQEYLEKRRSITNSALKDFLS-RANLNGDDDLDSNNS---SNGPRIGIAVSGGGYRA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 448520557 249 MLAGAGSILALDNRFEDSNTNALGGLLQASTYLVGLSGGSWMVGTLVLNDWISVENILNGSsqIWDLEASILDPNAGDLI 328
Cdd:cd07203   77 MLTGAGAIAAMDNRTDNATEHGLGGLLQSSTYLSGLSGGSWLVGSLASNNFTSVQDLLADS--IWNLDHSIFNPYGAAIV 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 448520557 329 ELARFYTGVGTAIVNKNRAGFNTSATDIWGRALSHQFLDDSSGGANLTWSSIRNLTSFKDHSMPYTILIANGKTVEAEVI 408
Cdd:cd07203  155 KTLNYYTNLANEVAQKKDAGFNVSLTDIWGRALSYQLFPALRGGPNLTWSSIRNQSWFQNAEMPFPIIVADGRYPGETII 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 448520557 409 SPNSTFIvEISPYELGNRD-ALNAFVDTEYLGSSLEDGDSH--QCVKNFDNAGFVMGTSSSVFNSVFSNLDDYDVSTVLR 485
Cdd:cd07203  235 NLNATVF-EFTPYEFGSWDpSLNSFTPTEYLGTNVSNGVPPngSCVNGFDNAGFVMGTSSTLFNQFLLQINSTSSPSFIK 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 448520557 486 PIFDQIMSVVSDTKDDVAVYKPNPFYETSYAQVDT---IINNNTLLLVDGGENGQNVPFYPLIQSDRGVDVILAFDNSAD 562
Cdd:cd07203  314 LIATGFLLDILKENQDIASYIPNPFQGYTYSNSNGtnpIVDSDYLDLVDGGEDGQNIPLWPLLQPERDVDVIFAFDSSAD 393
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 448520557 563 TKENWPNGTSFTETYKWQFTNQGK-GTPFPYVPTVDTYLSEDLKEKPIFFGCNASALSDivdfhndNDLNETDVPLVVYL 641
Cdd:cd07203  394 TDYNWPNGTSLVATYERQFSSQGNnGTGFPYVPDQNTFVNLGLNDRPTFFGCDGRNLTD-------LNVDQYTPPLVVYI 466
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 448520557 642 SNHHESYLSNFSTFKLAYDNAEKTGTIRNGYEVMSRGNLTDDSNWATCVGCAIIRRQQERLGEEQSEECAKCFQEYCWTG 721
Cdd:cd07203  467 PNAPWSYNSNISTFKLSYTDSERQGMILNGFESATRNNLTNDDEFATCVACAIIRRSLERLNITTPDECQQCFDNYCWNG 546

                 ....*.
gi 448520557 722 TAKDAP 727
Cdd:cd07203  547 TIDTTP 552
PLA2_B pfam01735
Lysophospholipase catalytic domain; This family consists of Lysophospholipase / phospholipase ...
237-722 2.96e-168

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 hydrolyzes 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: 496.89  E-value: 2.96e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 448520557  237 IGLAFSGGGYRAMLAGAGSILALDNRFEdsNTNALGGLLQASTYLVGLSGGSWMVGTLVLNDWISVENILN--GSSQIWD 314
Cdd:pfam01735   1 IGIAGSGGGYRAMLGGAGVLAALDNRTD--NETGLGGLLQSATYLAGLSGGSWLVGSLAVNNFTSVQDFPDkpEDISIWD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 448520557  315 LEASILDPNAGDLIELARFYTGVGTAIVNKNRAGFNTSATDIWGRALSHQFLDDSSGGANLTWSSIRNLTSFKDHSMPYT 394
Cdd:pfam01735  79 LNHSIFNPGGLNIPQNIKRYDDIVDAVWKKKNAGFNVSLTDIWGRALSYTLIPSLRGGPNYTWSSLRDAEWFQNAEMPFP 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 448520557  395 ILIANGKTVEAEVISPNSTfIVEISPYELGNRDA-LNAFVDTEYLGSSLEDG---DSHQCVKNFDNAGFVMGTSSSVFNS 470
Cdd:pfam01735 159 IIVADGRKPGTTVINLNAT-VFEFSPYEFGSWDPtLNSFTPTEYLGTKFFNGtpvKKGKCVPGFDNAGFVMGTSSTLFNQ 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 448520557  471 VFSNLDDYDVS-TVLRPIFDQIMSVVSDTKDDVAVYKPNPFYETSYAQVDT---IINNNTLLLVDGGENGQNVPFYPLIQ 546
Cdd:pfam01735 238 FLLVINSTSSLpSFLNIIIKHILKDLSEDSDDISQYPPNPFQDANDINQNAtnsIVDSDTLFLVDGGEDGQNIPLWPLLQ 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 448520557  547 SDRGVDVILAFDNSADTKENWPNGTSFTETYKWQF-TNQGKGTPFPYVPTVDTYLSEDLKEKPIFFGCNASALSDivdfh 625
Cdd:pfam01735 318 PERDVDVIFAVDNSADTDNDWPDGVSLVDTYERQFePLQVKGKKFPYVPDGNTFVNLGLNTRPTFFGCDARNLTD----- 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 448520557  626 NDNDLNETDVPLVVYLSNHHESYLSNFSTFKLAYDNAEKTGTIRNGYEVMSRGNLTDDSNWATCVGCAIIRRQQERLGEE 705
Cdd:pfam01735 393 LSARVSDSTPPLVVYLPNEPWSYMSNLSTFKISYNDSERQGLIENGFEAATQDNETDDPTFAHCVACAIIRRKLERLNIT 472
                         490
                  ....*....|....*..
gi 448520557  706 QSEECAKCFQEYCWTGT 722
Cdd:pfam01735 473 LPSECEQCFENYCWNGT 489
PLAc smart00022
Cytoplasmic phospholipase A2, catalytic subunit; Cytosolic phospholipases A2 hydrolyse ...
167-718 2.49e-158

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


Pssm-ID: 214474  Cd Length: 549  Bit Score: 473.84  E-value: 2.49e-158
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 448520557   167 NPYSPVNVTCPGD-VLVREGDGLSDNEKNYIEAKQEQTNKFLISFLNnRANlSNFDAESFINDNSDEhniTIGLAFSGGG 245
Cdd:smart00022  12 DSYAPYNVSCPSDiPLVRFSMGLSDNETEFLQKRKDYTNEAMKSFLG-RAN-SNFLDSSLLNSSDVP---KIAIAGSGGG 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 448520557   246 YRAMLAGAGSILALDNRfedSNTNALGGLLQASTYLVGLSGGSWMVGTLVLNDWISVENILNgSSQIWDLEASILDPNAg 325
Cdd:smart00022  87 FRAMVGGAGVLKAMDNR---TDGHGLGGLLQSATYLAGLSGGTWLVGTLASNNFTPVKGPEE-INSEWMFSVSINNPGI- 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 448520557   326 DLIELARFYTGVGTAIVNKNRAGFNTSATDIWGRALSHQFlDDSSGGANLTWSSIRNLTSFKDHSMPYTILIANGKTVEA 405
Cdd:smart00022 162 NLLLTAQFYKSIVDAVWKKKDAGFNISLTDIWGRALSYNL-FDSLGGPNYTLSSLRDQEKFQNAEMPLPIFVADGRKPGE 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 448520557   406 EVISPNSTFiVEISPYELGNRDA-LNAFVDTEYLGSSLEDG---DSHQCVKNFDNAGFVMGTSSSVFNSVFSNLDDY-DV 480
Cdd:smart00022 241 SVINFNDTV-FEFSPFEFGSWDPkLNAFMPPEYLGSKFFNGtpvKKGKCIPNFDNAGFIMGTSSSLFNRFLLVLSNStME 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 448520557   481 STVLRPIFDQIMSVVSDTKDDVAVYKPNPFYETSYAQVD---TIINNNTLLLVDGGENGQNVPFYPLIQSDRGVDVILAF 557
Cdd:smart00022 320 ESLIKIIIKHILKDLSSDSDDIAIYPPNPFKDDAYVQRMltnSLGDSDLLNLVDGGEDGENIPLSPLLQPERSVDVIFAV 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 448520557   558 DNSADTKENWPNGTSFTETYKWQFTNQGK--GTPFPYVPTVDTYLSEDLKEKPIFFGCNASALSDIVdfhndndlnetdv 635
Cdd:smart00022 400 DASADTDEFWPNGSSLVKTYERHVVDQGLtfNLPFPYVPDTQTFVNLGLSTKPTFFGCDSSNLTYIP------------- 466
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 448520557   636 PLVVYLSNHHESYLSNFSTFKLAYDNAEKTGTIRNGYEVMSRGNLTDDSNWATCVGCAIIRRQQERLGEEQSEECAKCFQ 715
Cdd:smart00022 467 PLVVYLPNEKWAYNSNISTFKISYSVFEREGLIKNGYEFATVNNSTDDDCFIHCVACAIIFRKQEAPNVTLPSECSKCFY 546

                   ...
gi 448520557   716 EYC 718
Cdd:smart00022 547 NYC 549
 
Name Accession Description Interval E-value
cPLA2_Fungal_PLB cd07203
Fungal Phospholipase B-like; cPLA2 GrpIVA homologs; catalytic domain; Fungal phospholipase B ...
171-727 0e+00

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: 618.61  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 448520557 171 PVNVTCPGDV-LVREG-DGLSDNEKNYIEAKQEQTNKFLISFLNnRANLSNFDAESFINDnsdEHNITIGLAFSGGGYRA 248
Cdd:cd07203    1 PFNVSCPSDAnLIRSAsDGLSTNEQEYLEKRRSITNSALKDFLS-RANLNGDDDLDSNNS---SNGPRIGIAVSGGGYRA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 448520557 249 MLAGAGSILALDNRFEDSNTNALGGLLQASTYLVGLSGGSWMVGTLVLNDWISVENILNGSsqIWDLEASILDPNAGDLI 328
Cdd:cd07203   77 MLTGAGAIAAMDNRTDNATEHGLGGLLQSSTYLSGLSGGSWLVGSLASNNFTSVQDLLADS--IWNLDHSIFNPYGAAIV 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 448520557 329 ELARFYTGVGTAIVNKNRAGFNTSATDIWGRALSHQFLDDSSGGANLTWSSIRNLTSFKDHSMPYTILIANGKTVEAEVI 408
Cdd:cd07203  155 KTLNYYTNLANEVAQKKDAGFNVSLTDIWGRALSYQLFPALRGGPNLTWSSIRNQSWFQNAEMPFPIIVADGRYPGETII 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 448520557 409 SPNSTFIvEISPYELGNRD-ALNAFVDTEYLGSSLEDGDSH--QCVKNFDNAGFVMGTSSSVFNSVFSNLDDYDVSTVLR 485
Cdd:cd07203  235 NLNATVF-EFTPYEFGSWDpSLNSFTPTEYLGTNVSNGVPPngSCVNGFDNAGFVMGTSSTLFNQFLLQINSTSSPSFIK 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 448520557 486 PIFDQIMSVVSDTKDDVAVYKPNPFYETSYAQVDT---IINNNTLLLVDGGENGQNVPFYPLIQSDRGVDVILAFDNSAD 562
Cdd:cd07203  314 LIATGFLLDILKENQDIASYIPNPFQGYTYSNSNGtnpIVDSDYLDLVDGGEDGQNIPLWPLLQPERDVDVIFAFDSSAD 393
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 448520557 563 TKENWPNGTSFTETYKWQFTNQGK-GTPFPYVPTVDTYLSEDLKEKPIFFGCNASALSDivdfhndNDLNETDVPLVVYL 641
Cdd:cd07203  394 TDYNWPNGTSLVATYERQFSSQGNnGTGFPYVPDQNTFVNLGLNDRPTFFGCDGRNLTD-------LNVDQYTPPLVVYI 466
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 448520557 642 SNHHESYLSNFSTFKLAYDNAEKTGTIRNGYEVMSRGNLTDDSNWATCVGCAIIRRQQERLGEEQSEECAKCFQEYCWTG 721
Cdd:cd07203  467 PNAPWSYNSNISTFKLSYTDSERQGMILNGFESATRNNLTNDDEFATCVACAIIRRSLERLNITTPDECQQCFDNYCWNG 546

                 ....*.
gi 448520557 722 TAKDAP 727
Cdd:cd07203  547 TIDTTP 552
PLA2_B pfam01735
Lysophospholipase catalytic domain; This family consists of Lysophospholipase / phospholipase ...
237-722 2.96e-168

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 hydrolyzes 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: 496.89  E-value: 2.96e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 448520557  237 IGLAFSGGGYRAMLAGAGSILALDNRFEdsNTNALGGLLQASTYLVGLSGGSWMVGTLVLNDWISVENILN--GSSQIWD 314
Cdd:pfam01735   1 IGIAGSGGGYRAMLGGAGVLAALDNRTD--NETGLGGLLQSATYLAGLSGGSWLVGSLAVNNFTSVQDFPDkpEDISIWD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 448520557  315 LEASILDPNAGDLIELARFYTGVGTAIVNKNRAGFNTSATDIWGRALSHQFLDDSSGGANLTWSSIRNLTSFKDHSMPYT 394
Cdd:pfam01735  79 LNHSIFNPGGLNIPQNIKRYDDIVDAVWKKKNAGFNVSLTDIWGRALSYTLIPSLRGGPNYTWSSLRDAEWFQNAEMPFP 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 448520557  395 ILIANGKTVEAEVISPNSTfIVEISPYELGNRDA-LNAFVDTEYLGSSLEDG---DSHQCVKNFDNAGFVMGTSSSVFNS 470
Cdd:pfam01735 159 IIVADGRKPGTTVINLNAT-VFEFSPYEFGSWDPtLNSFTPTEYLGTKFFNGtpvKKGKCVPGFDNAGFVMGTSSTLFNQ 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 448520557  471 VFSNLDDYDVS-TVLRPIFDQIMSVVSDTKDDVAVYKPNPFYETSYAQVDT---IINNNTLLLVDGGENGQNVPFYPLIQ 546
Cdd:pfam01735 238 FLLVINSTSSLpSFLNIIIKHILKDLSEDSDDISQYPPNPFQDANDINQNAtnsIVDSDTLFLVDGGEDGQNIPLWPLLQ 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 448520557  547 SDRGVDVILAFDNSADTKENWPNGTSFTETYKWQF-TNQGKGTPFPYVPTVDTYLSEDLKEKPIFFGCNASALSDivdfh 625
Cdd:pfam01735 318 PERDVDVIFAVDNSADTDNDWPDGVSLVDTYERQFePLQVKGKKFPYVPDGNTFVNLGLNTRPTFFGCDARNLTD----- 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 448520557  626 NDNDLNETDVPLVVYLSNHHESYLSNFSTFKLAYDNAEKTGTIRNGYEVMSRGNLTDDSNWATCVGCAIIRRQQERLGEE 705
Cdd:pfam01735 393 LSARVSDSTPPLVVYLPNEPWSYMSNLSTFKISYNDSERQGLIENGFEAATQDNETDDPTFAHCVACAIIRRKLERLNIT 472
                         490
                  ....*....|....*..
gi 448520557  706 QSEECAKCFQEYCWTGT 722
Cdd:pfam01735 473 LPSECEQCFENYCWNGT 489
PLAc smart00022
Cytoplasmic phospholipase A2, catalytic subunit; Cytosolic phospholipases A2 hydrolyse ...
167-718 2.49e-158

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


Pssm-ID: 214474  Cd Length: 549  Bit Score: 473.84  E-value: 2.49e-158
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 448520557   167 NPYSPVNVTCPGD-VLVREGDGLSDNEKNYIEAKQEQTNKFLISFLNnRANlSNFDAESFINDNSDEhniTIGLAFSGGG 245
Cdd:smart00022  12 DSYAPYNVSCPSDiPLVRFSMGLSDNETEFLQKRKDYTNEAMKSFLG-RAN-SNFLDSSLLNSSDVP---KIAIAGSGGG 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 448520557   246 YRAMLAGAGSILALDNRfedSNTNALGGLLQASTYLVGLSGGSWMVGTLVLNDWISVENILNgSSQIWDLEASILDPNAg 325
Cdd:smart00022  87 FRAMVGGAGVLKAMDNR---TDGHGLGGLLQSATYLAGLSGGTWLVGTLASNNFTPVKGPEE-INSEWMFSVSINNPGI- 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 448520557   326 DLIELARFYTGVGTAIVNKNRAGFNTSATDIWGRALSHQFlDDSSGGANLTWSSIRNLTSFKDHSMPYTILIANGKTVEA 405
Cdd:smart00022 162 NLLLTAQFYKSIVDAVWKKKDAGFNISLTDIWGRALSYNL-FDSLGGPNYTLSSLRDQEKFQNAEMPLPIFVADGRKPGE 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 448520557   406 EVISPNSTFiVEISPYELGNRDA-LNAFVDTEYLGSSLEDG---DSHQCVKNFDNAGFVMGTSSSVFNSVFSNLDDY-DV 480
Cdd:smart00022 241 SVINFNDTV-FEFSPFEFGSWDPkLNAFMPPEYLGSKFFNGtpvKKGKCIPNFDNAGFIMGTSSSLFNRFLLVLSNStME 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 448520557   481 STVLRPIFDQIMSVVSDTKDDVAVYKPNPFYETSYAQVD---TIINNNTLLLVDGGENGQNVPFYPLIQSDRGVDVILAF 557
Cdd:smart00022 320 ESLIKIIIKHILKDLSSDSDDIAIYPPNPFKDDAYVQRMltnSLGDSDLLNLVDGGEDGENIPLSPLLQPERSVDVIFAV 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 448520557   558 DNSADTKENWPNGTSFTETYKWQFTNQGK--GTPFPYVPTVDTYLSEDLKEKPIFFGCNASALSDIVdfhndndlnetdv 635
Cdd:smart00022 400 DASADTDEFWPNGSSLVKTYERHVVDQGLtfNLPFPYVPDTQTFVNLGLSTKPTFFGCDSSNLTYIP------------- 466
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 448520557   636 PLVVYLSNHHESYLSNFSTFKLAYDNAEKTGTIRNGYEVMSRGNLTDDSNWATCVGCAIIRRQQERLGEEQSEECAKCFQ 715
Cdd:smart00022 467 PLVVYLPNEKWAYNSNISTFKISYSVFEREGLIKNGYEFATVNNSTDDDCFIHCVACAIIFRKQEAPNVTLPSECSKCFY 546

                   ...
gi 448520557   716 EYC 718
Cdd:smart00022 547 NYC 549
cPLA2_like cd00147
Cytosolic phospholipase A2, catalytic domain; hydrolyses arachidonyl phospholipids; Catalytic ...
182-691 1.01e-114

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: 356.56  E-value: 1.01e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 448520557 182 VREGDGLSDNEKNYIEAKQEQTNKFLISFLNNRanlsnfdaesfiNDNSDEHNITIGLAFSGGGYRAMLAGAGSILALDN 261
Cdd:cd00147    1 VRLASDLCDEEKEFLEKRRKVVAKALKKFLGLE------------NDLNPDEVPVIAILGSGGGYRAMTGGAGALKALDE 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 448520557 262 rfedsntnalGGLLQASTYLVGLSGGSWMVGTLVLNDWISVENIlnGSSQIWDLEASILDPNagdLIELARFYTGVGTAI 341
Cdd:cd00147   69 ----------GGLLDCVTYLSGLSGSTWLMASLYSNPDWSQKDL--DEAIEWLKRHVIKSPL---LLFSPERLKYYAKEL 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 448520557 342 VNKNRAGFNTSATDIWGRALSHQFLDdssggaNLTWSSIRNLTSF-KDHSMPYTILIANGKTVEAEVISPNSTfIVEISP 420
Cdd:cd00147  134 EEKKKAGFNVSLTDFWGLLLGYTLLK------ELTDSSLSDQREFvQNGQNPLPIYTALNVKPGETSINDFAT-WFEFTP 206
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 448520557 421 YELGNRDaLNAFVDTEYLGSSLEDGDSHQcVKNFDNAGFVMGTsssvfnsvfsnlddydVSTVLRPIFDQIMSVvsdtkd 500
Cdd:cd00147  207 YEVGFPK-YGAFIPTEYFGSKFFMGRLVK-KIPEDRLGFLMGT----------------WGSAFSIILLDAGKY------ 262
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 448520557 501 dvavykPNPFYETSYAQVDTIINNN------TLLLVDGGENGQNVPFYPLIQSDRGVDVILAFDNSADTKeNWPNGTSFT 574
Cdd:cd00147  263 ------PNFFYGLNLHKSYLRSPNPlitssdTLHLVDAGLDINNIPLPPLLRPERDVDVILSFDFSADDP-DWPNGLKLV 335
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 448520557 575 ETY-KWQFTNqgkGTPFPYVPTVDTYLSEDLKEKPIFFGCNAsalsdivdfhndndlneTDVPLVVYLSN--------HH 645
Cdd:cd00147  336 ATYeRQASSN---GIPFPKIPDSVTFDNLGLKECYVFFGCDD-----------------PDAPLVVYFPLvndtfrkyDF 395
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*.
gi 448520557 646 ESYLSNFSTFKLAYDNAEKTGTIRNGYEVMSRgnlTDDSNWATCVG 691
Cdd:cd00147  396 DDPNSPYSTFNLSYTDEEFDRLLELAFYNVTN---NKDTILQALRA 438
cPLA2_Grp-IVA cd07200
Group IVA cytosolic phospholipase A2; catalytic domain; Ca-dependent; Group IVA cPLA2, an 85 ...
183-663 3.71e-14

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: 75.95  E-value: 3.71e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 448520557 183 REGDGLSDNEKNYIEAKQEQTNKFLISFLNnranlsnfdAESFINDNSDEhNITIGLAFSGGGYRAMLAGAGSILAldnr 262
Cdd:cd07200    2 RFSMALCDEEKEFRQARKMRVREALRKLLG---------EEGPKVTSLRE-VPVIALLGSGGGFRAMVGMSGAMKA---- 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 448520557 263 FEDSntnalgGLLQASTYLVGLSGGSWMVGTL-VLNDWISVE------NILNGSSQIWdleASILDPnagdliELARFYT 335
Cdd:cd07200   68 LYDS------GVLDCATYVAGLSGSTWYMSTLySHPDFPEKGpgeinkELMRNVSSSP---LLLLTP------QLLKRYT 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 448520557 336 gvgTAIVNKNRAGFNTSATDIWGRALSHQFLDDSsgganlTWSSIRNLTSF-KDHSMPYTILIAngKTVEAEVisPNSTF 414
Cdd:cd07200  133 ---EALWEKKSSGQPVTFTDFFGMLIGETLIKER------MDTKLSDLQEKvNDGQVPLPLFTC--LHVKPDV--SALMF 199
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 448520557 415 --IVEISPYELGnRDALNAFVDTEYLGSSLEDGdshQCVKNFDNA--GFVMGTSSSVFNSVFSNLDDYdVSTVLRP--IF 488
Cdd:cd07200  200 hdWVEFSPYEIG-MAKYGTFMSPDLFGSKFFMG---FLAKKYPENplHFLMGVWGSAFSILFNRVLGR-NSREGRAgkVH 274
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 448520557 489 DQIMSVVSDTkddvaVYKPNPFYETSYAQVDTII---------------NNNTLLLVDGGeNGQNVPfYPLIQ-SDRGVD 552
Cdd:cd07200  275 NFMLGLNLNT-----SYPLSPLSDLATDEPEAAVadadeferiyepldtKSKKIHVVDSG-LTFNLP-YPLILrPQRGVD 347
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 448520557 553 VILAFDNSADTKENWPNGTSFTETYKWQFTNqgkGTPFPYVPTvDTYLSEDLKEKPIFfgcnasalsdivdfhndNDLNE 632
Cdd:cd07200  348 LIISFDFSARPSDSSPPFKELLLAEKWARMN---GLPFPPIDF-KVFDREGLKECYVF-----------------KPKND 406
                        490       500       510
                 ....*....|....*....|....*....|...
gi 448520557 633 TDVPLVVY--LSNHHesyLSNFSTFKLAYDNAE 663
Cdd:cd07200  407 DDCPTVIHfvLCNIN---FRNLKAPGVPRETEE 436
cPLA2_Grp-IVC cd07202
Group IVC cytoplasmic phospholipase A2; catalytic domain; Ca-independent; Group IVC cPLA2, a ...
182-445 4.74e-10

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  Cd Length: 430  Bit Score: 62.50  E-value: 4.74e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 448520557 182 VREGDGLSDNEKNYIEAKQEqtnkfliSFLNNRANLsnfdaesfiNDNSDEHNItIGLAFSGGGYRAMLAGAGSILALDN 261
Cdd:cd07202    3 VRIAPGLNKEEKAAVVKRRK-------DVLQSLQKL---------GINADKAPV-IAVLGSGGGLRAMIACLGVLSELDK 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 448520557 262 RfedsntnalgGLLQASTYLVGLSGGSWMVGTL-VLNDWIS----VENIL--NGSSQIWDLEASILdpnagDLIELARFY 334
Cdd:cd07202   66 A----------GLLDCVTYLAGVSGSTWCMSSLyTEPDWSTklqtVEDELkrRLQKVSWDFAYALK-----KEIQAAKSD 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 448520557 335 tgvgtaivnknragfNTSATDIWGRALSHQF---LDDSsgganltwssirNLTSFKDHS----MPYTILIANGKTVEA-- 405
Cdd:cd07202  131 ---------------NFSLTDFWAYLVVTTFtkeLDES------------TLSDQRKQSeegkDPYPIFAAIDKDLSEwk 183
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 448520557 406 EVISPNSTFivEISPYELGnRDALNAFVDTEYLGSSLEDG 445
Cdd:cd07202  184 ERKTGDPWF--EFTPHEAG-YPLPGAFVSTTHFGSKFENG 220
cPLA2_Grp-IVB-IVD-IVE-IVF cd07201
Group IVB, IVD, IVE, and IVF cytosolic phospholipase A2; catalytic domain; Ca-dependent; Group ...
176-440 1.18e-06

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: 51.95  E-value: 1.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 448520557 176 CPGDVLVREGDGLSDNEKNYIEAKQEQTNKFLISFLNNRANLsnfdaesfindnsDEHNI-TIGLAFSGGGYRAMLAGAG 254
Cdd:cd07201    6 SSEDLDVRLGFDLCAEEQEFLQKRKKVVAAALKKALQLEEDL-------------QEDEVpVVAVMTTGGGTRALTSMYG 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 448520557 255 SILALDNRfedsntnalgGLLQASTYLVGLSGGSWMVGTLVLN-DWisvenilngsSQIwDLEASILDPN---------A 324
Cdd:cd07201   73 SLLGLQKL----------GLLDCVSYITGLSGSTWTMATLYEDpNW----------SQK-DLEGPIEEARkhvtksklgC 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 448520557 325 GDLIELARFYTGVGTaivnKNRAGFNTSATDIWGRALSHqFLDDSSGGANLtwSSIRNLTSFKDHSMP-YTILIANGKTv 403
Cdd:cd07201  132 FSPERLKYYRQELSE----REQEGHKVSFIDLWGLIIES-MLHDKKNDHKL--SDQREAVSQGQNPLPiYLSLNVKDNL- 203
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 448520557 404 eaevispnSTF----IVEISPYELGNRDaLNAFVDTEYLGS 440
Cdd:cd07201  204 --------STQdfreWVEFTPYEVGFLK-YGAFIPAEDFGS 235
Patatin_and_cPLA2 cd01819
Patatins and Phospholipases; Patatin-like phospholipase. This family consists of various ...
239-294 1.00e-05

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: 46.25  E-value: 1.00e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 448520557 239 LAFSGGGYRAMlAGAGSILALDNRfedsntnalgGLLQASTYLVGLSGGSWMVGTL 294
Cdd:cd01819    1 LSFSGGGFRGM-YHAGVLSALAER----------GLLDCVTYLAGTSGGAWVAATL 45
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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