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Conserved domains on  [gi|1134785751|gb|APX53423|]
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phospholipase B 1, partial [Cryptococcus neoformans var. grubii]

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 ...
 1-123 9.30e-51

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: 168.31  E-value: 9.30e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134785751   1 VTWIRNATTGLGSGERAYIEAREKLVQPVIEQMMAARGLE--------TPPRTPNIGVALAGGGYRAMLTGLGGIMGMMN 72
Cdd:cd07203    10 ANLIRSASDGLSTNEQEYLEKRRSITNSALKDFLSRANLNgdddldsnNSSNGPRIGIAVSGGGYRAMLTGAGAIAAMDN 89

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1134785751  73 ESTEASESETGGWLDGVSYWAGLSGGSWATGTFMSNGGQLPTNLL-ENLWNI 123
Cdd:cd07203    90 RTDNATEHGLGGLLQSSTYLSGLSGGSWLVGSLASNNFTSVQDLLaDSIWNL 141
 
Name Accession Description Interval E-value
cPLA2_Fungal_PLB cd07203
Fungal Phospholipase B-like; cPLA2 GrpIVA homologs; catalytic domain; Fungal phospholipase B ...
 1-123 9.30e-51

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: 168.31  E-value: 9.30e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134785751   1 VTWIRNATTGLGSGERAYIEAREKLVQPVIEQMMAARGLE--------TPPRTPNIGVALAGGGYRAMLTGLGGIMGMMN 72
Cdd:cd07203    10 ANLIRSASDGLSTNEQEYLEKRRSITNSALKDFLSRANLNgdddldsnNSSNGPRIGIAVSGGGYRAMLTGAGAIAAMDN 89

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1134785751  73 ESTEASESETGGWLDGVSYWAGLSGGSWATGTFMSNGGQLPTNLL-ENLWNI 123
Cdd:cd07203    90 RTDNATEHGLGGLLQSSTYLSGLSGGSWLVGSLASNNFTSVQDLLaDSIWNL 141
PLAc smart00022
Cytoplasmic phospholipase A2, catalytic subunit; Cytosolic phospholipases A2 hydrolyse ...
 4-123 2.98e-17

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


Pssm-ID: 214474  Cd Length: 549  Bit Score: 75.93  E-value: 2.98e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134785751    4 IRNATtGLGSGERAYIEAREKLVQpviEQMMAARGLETPP----------RTPNIGVALAGGGYRAMLTGlGGIMGMMNE 73
Cdd:smart00022  28 VRFSM-GLSDNETEFLQKRKDYTN---EAMKSFLGRANSNfldssllnssDVPKIAIAGSGGGFRAMVGG-AGVLKAMDN 102

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1134785751   74 STEAseSETGGWLDGVSYWAGLSGGSWATGTFMSNGGQLPTNLLE--NLWNI 123
Cdd:smart00022 103 RTDG--HGLGGLLQSATYLAGLSGGTWLVGTLASNNFTPVKGPEEinSEWMF 152
PLA2_B pfam01735
Lysophospholipase catalytic domain; This family consists of Lysophospholipase / phospholipase ...
 48-123 7.67e-15

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: 69.32  E-value: 7.67e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134785751  48 IGVALAGGGYRAMLTGlGGIMGMMNESTEASESEtGGWLDGVSYWAGLSGGSWATGTFMSNGGQLPTNLLE-----NLWN 122
Cdd:pfam01735   1 IGIAGSGGGYRAMLGG-AGVLAALDNRTDNETGL-GGLLQSATYLAGLSGGSWLVGSLAVNNFTSVQDFPDkpediSIWD 78


                  .
gi 1134785751 123 I 123
Cdd:pfam01735  79 L 79
 
Name Accession Description Interval E-value
cPLA2_Fungal_PLB cd07203
Fungal Phospholipase B-like; cPLA2 GrpIVA homologs; catalytic domain; Fungal phospholipase B ...
 1-123 9.30e-51

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: 168.31  E-value: 9.30e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134785751   1 VTWIRNATTGLGSGERAYIEAREKLVQPVIEQMMAARGLE--------TPPRTPNIGVALAGGGYRAMLTGLGGIMGMMN 72
Cdd:cd07203    10 ANLIRSASDGLSTNEQEYLEKRRSITNSALKDFLSRANLNgdddldsnNSSNGPRIGIAVSGGGYRAMLTGAGAIAAMDN 89

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1134785751  73 ESTEASESETGGWLDGVSYWAGLSGGSWATGTFMSNGGQLPTNLL-ENLWNI 123
Cdd:cd07203    90 RTDNATEHGLGGLLQSSTYLSGLSGGSWLVGSLASNNFTSVQDLLaDSIWNL 141
cPLA2_like cd00147
Cytosolic phospholipase A2, catalytic domain; hydrolyses arachidonyl phospholipids; Catalytic ...
 4-123 1.20e-31

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: 115.81  E-value: 1.20e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134785751   4 IRNATtGLGSGERAYIEAREKLVQPVIEQMMAARGLETPPRTPNIGVALAGGGYRAMLTGLGGIMGMMNesteasesetG 83
Cdd:cd00147     1 VRLAS-DLCDEEKEFLEKRRKVVAKALKKFLGLENDLNPDEVPVIAILGSGGGYRAMTGGAGALKALDE----------G 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1134785751  84 GWLDGVSYWAGLSGGSWATGTFMSNGGQLPTNLLE-NLWNI 123
Cdd:cd00147    70 GLLDCVTYLSGLSGSTWLMASLYSNPDWSQKDLDEaIEWLK 110
PLAc smart00022
Cytoplasmic phospholipase A2, catalytic subunit; Cytosolic phospholipases A2 hydrolyse ...
 4-123 2.98e-17

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


Pssm-ID: 214474  Cd Length: 549  Bit Score: 75.93  E-value: 2.98e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134785751    4 IRNATtGLGSGERAYIEAREKLVQpviEQMMAARGLETPP----------RTPNIGVALAGGGYRAMLTGlGGIMGMMNE 73
Cdd:smart00022  28 VRFSM-GLSDNETEFLQKRKDYTN---EAMKSFLGRANSNfldssllnssDVPKIAIAGSGGGFRAMVGG-AGVLKAMDN 102

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1134785751   74 STEAseSETGGWLDGVSYWAGLSGGSWATGTFMSNGGQLPTNLLE--NLWNI 123
Cdd:smart00022 103 RTDG--HGLGGLLQSATYLAGLSGGTWLVGTLASNNFTPVKGPEEinSEWMF 152
PLA2_B pfam01735
Lysophospholipase catalytic domain; This family consists of Lysophospholipase / phospholipase ...
 48-123 7.67e-15

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: 69.32  E-value: 7.67e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134785751  48 IGVALAGGGYRAMLTGlGGIMGMMNESTEASESEtGGWLDGVSYWAGLSGGSWATGTFMSNGGQLPTNLLE-----NLWN 122
Cdd:pfam01735   1 IGIAGSGGGYRAMLGG-AGVLAALDNRTDNETGL-GGLLQSATYLAGLSGGSWLVGSLAVNNFTSVQDFPDkpediSIWD 78


                  .
gi 1134785751 123 I 123
Cdd:pfam01735  79 L 79
cPLA2_Grp-IVA cd07200
Group IVA cytosolic phospholipase A2; catalytic domain; Ca-dependent; Group IVA cPLA2, an 85 ...
 11-110 8.33e-11

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: 57.84  E-value: 8.33e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134785751  11 LGSGERAYIEAREKLVQPVIEQMMaarGLETPPR-----TPNIGVALAGGGYRAMlTGLGGIMGMMNESteasesetgGW 85
Cdd:cd07200     7 LCDEEKEFRQARKMRVREALRKLL---GEEGPKVtslreVPVIALLGSGGGFRAM-VGMSGAMKALYDS---------GV 73

                          90       100
                  ....*....|....*....|....*
gi 1134785751  86 LDGVSYWAGLSGGSWATGTFMSNGG 110
Cdd:cd07200    74 LDCATYVAGLSGSTWYMSTLYSHPD 98
cPLA2_Grp-IVC cd07202
Group IVC cytoplasmic phospholipase A2; catalytic domain; Ca-independent; Group IVC cPLA2, a ...
 9-101 2.38e-09

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: 53.64  E-value: 2.38e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134785751   9 TGLGSGERAYIEAREKLVQpvieQMMAARGLETPpRTPNIGVALAGGGYRAMLtGLGGIMGMMNESteasesetgGWLDG 88
Cdd:cd07202     7 PGLNKEEKAAVVKRRKDVL----QSLQKLGINAD-KAPVIAVLGSGGGLRAMI-ACLGVLSELDKA---------GLLDC 71

                          90
                  ....*....|...
gi 1134785751  89 VSYWAGLSGGSWA 101
Cdd:cd07202    72 VTYLAGVSGSTWC 84
cPLA2_Grp-IVB-IVD-IVE-IVF cd07201
Group IVB, IVD, IVE, and IVF cytosolic phospholipase A2; catalytic domain; Ca-dependent; Group ...
 10-101 1.08e-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: 45.79  E-value: 1.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134785751  10 GLGSGERAYIEAREKLVQPVIEQMMAARGLETPPRTPNIGVALAGGGYRAMLTGLGGIMGMMNEsteasesetgGWLDGV 89
Cdd:cd07201    17 DLCAEEQEFLQKRKKVVAAALKKALQLEEDLQEDEVPVVAVMTTGGGTRALTSMYGSLLGLQKL----------GLLDCV 86

                          90
                  ....*....|..
gi 1134785751  90 SYWAGLSGGSWA 101
Cdd:cd07201    87 SYITGLSGSTWT 98
Patatin_and_cPLA2 cd01819
Patatins and Phospholipases; Patatin-like phospholipase. This family consists of various ...
 50-121 9.06e-03

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: 33.93  E-value: 9.06e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1134785751  50 VALAGGGYRAMltGLGGIMGMMNESteasesetgGWLDGVSYWAGLSGGSWATGTFM---SNGGQLPTNLLENLW 121
Cdd:cd01819     1 LSFSGGGFRGM--YHAGVLSALAER---------GLLDCVTYLAGTSGGAWVAATLYppsSSLDNKPRQSLEEAL 64
 
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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