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Conserved domains on  [gi|2024468187|ref|XP_040518931|]
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otoconin-90 isoform X5 [Gallus gallus]

Protein Classification

otoconin_90 domain-containing protein( domain architecture ID 10140446)

otoconin_90 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
otoconin_90 cd04707
otoconin_90: Phospholipase A2-like domains present in otoconin-90 and otoconin-95, mammal ...
 353-469 2.83e-58

otoconin_90: Phospholipase A2-like domains present in otoconin-90 and otoconin-95, mammal proteins that are principal matrix proteins of calcitic otoconia. Interactions involving otoconin-90 may trigger or constitute key events in otoconia formation. The PLA2-like domains in otoconins may have lost their metal-binding sites.


:

Pssm-ID: 153096  Cd Length: 117  Bit Score: 189.22  E-value: 2.83e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024468187 353 QLGEMLFCLTERCPEEFESYGCYCGQEGRGHPTDALDRCCFSHHCCVEQVKTLGCPAERSSRSEVVCFDHMPKCIGWSLC 432
Cdd:cd04707     1 QLGEMLKCLTGRCPREFEDYGCYCGQEGEGLPVDELDRCCFQHRCCLEQASEMGCLQDRKLSTEVTCVDHKPKCEGVSVC 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2024468187 433 EKLLCACDQTAAQCMASALFNESLKFPHGQVCQEEKA 469
Cdd:cd04707    81 EKLLCTCDKTAAECMAAAHFNSSLNSLDVSSCPGQVP 117
otoconin_90 cd04707
otoconin_90: Phospholipase A2-like domains present in otoconin-90 and otoconin-95, mammal ...
 80-197 1.98e-53

otoconin_90: Phospholipase A2-like domains present in otoconin-90 and otoconin-95, mammal proteins that are principal matrix proteins of calcitic otoconia. Interactions involving otoconin-90 may trigger or constitute key events in otoconia formation. The PLA2-like domains in otoconins may have lost their metal-binding sites.


:

Pssm-ID: 153096  Cd Length: 117  Bit Score: 176.51  E-value: 1.98e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024468187  80 NFVNKMKCVSGFCPRDFEDYGCSCRFEMEGLPVDEADECCFQHRKCYEEAMEMECTWDpSKISTDVTCSAENLSCENGDP 159
Cdd:cd04707     1 QLGEMLKCLTGRCPREFEDYGCYCGQEGEGLPVDELDRCCFQHRCCLEQASEMGCLQD-RKLSTEVTCVDHKPKCEGVSV 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2024468187 160 CEQFLCTCDKDAIECFGNAHINSSLNGLDVSSCPSLVT 197
Cdd:cd04707    80 CEKLLCTCDKTAAECMAAAHFNSSLNSLDVSSCPGQVP 117
 
Name Accession Description Interval E-value
otoconin_90 cd04707
otoconin_90: Phospholipase A2-like domains present in otoconin-90 and otoconin-95, mammal ...
 353-469 2.83e-58

otoconin_90: Phospholipase A2-like domains present in otoconin-90 and otoconin-95, mammal proteins that are principal matrix proteins of calcitic otoconia. Interactions involving otoconin-90 may trigger or constitute key events in otoconia formation. The PLA2-like domains in otoconins may have lost their metal-binding sites.


Pssm-ID: 153096  Cd Length: 117  Bit Score: 189.22  E-value: 2.83e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024468187 353 QLGEMLFCLTERCPEEFESYGCYCGQEGRGHPTDALDRCCFSHHCCVEQVKTLGCPAERSSRSEVVCFDHMPKCIGWSLC 432
Cdd:cd04707     1 QLGEMLKCLTGRCPREFEDYGCYCGQEGEGLPVDELDRCCFQHRCCLEQASEMGCLQDRKLSTEVTCVDHKPKCEGVSVC 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2024468187 433 EKLLCACDQTAAQCMASALFNESLKFPHGQVCQEEKA 469
Cdd:cd04707    81 EKLLCTCDKTAAECMAAAHFNSSLNSLDVSSCPGQVP 117
otoconin_90 cd04707
otoconin_90: Phospholipase A2-like domains present in otoconin-90 and otoconin-95, mammal ...
 80-197 1.98e-53

otoconin_90: Phospholipase A2-like domains present in otoconin-90 and otoconin-95, mammal proteins that are principal matrix proteins of calcitic otoconia. Interactions involving otoconin-90 may trigger or constitute key events in otoconia formation. The PLA2-like domains in otoconins may have lost their metal-binding sites.


Pssm-ID: 153096  Cd Length: 117  Bit Score: 176.51  E-value: 1.98e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024468187  80 NFVNKMKCVSGFCPRDFEDYGCSCRFEMEGLPVDEADECCFQHRKCYEEAMEMECTWDpSKISTDVTCSAENLSCENGDP 159
Cdd:cd04707     1 QLGEMLKCLTGRCPREFEDYGCYCGQEGEGLPVDELDRCCFQHRCCLEQASEMGCLQD-RKLSTEVTCVDHKPKCEGVSV 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2024468187 160 CEQFLCTCDKDAIECFGNAHINSSLNGLDVSSCPSLVT 197
Cdd:cd04707    80 CEKLLCTCDKTAAECMAAAHFNSSLNSLDVSSCPGQVP 117
Phospholip_A2_1 pfam00068
Phospholipase A2; Phospholipase A2 releases fatty acids from the second carbon group of ...
 351-457 1.36e-41

Phospholipase A2; Phospholipase A2 releases fatty acids from the second carbon group of glycerol. Perhaps the best known members are secreted snake venoms, but also found in secreted pancreatic and membrane-associated forms. Structure is all-alpha, with two core disulfide-linked helices and a calcium-binding loop. This alignment represents the major family of PLA2s. A second minor family, defined by the honeybee venom PLA2 PDB:1POC and related sequences from Gila monsters (Heloderma), is not recognized. This minor family conserves the core helix pair but is substantially different elsewhere. The PROSITE pattern PA2_HIS, specific to the first core helix, recognizes both families.


Pssm-ID: 459659  Cd Length: 108  Bit Score: 144.67  E-value: 1.36e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024468187 351 LPQLGEMLFCLTER-CPEEFESYGCYCGQEGRGHPTDALDRCCFSHHCCVEQVKTLGCPAERSSRSEVVCFDHMPKCIGW 429
Cdd:pfam00068   1 LWQFGEMIKCTTGRnPPLDYNDYGCYCGLGGSGTPVDATDRCCQAHDCCYERLKKLGCGNPYLLSYNYSCSDGTITCSGN 80

                          90       100
                  ....*....|....*....|....*...
gi 2024468187 430 SLCEKLLCACDQTAAQCMASALFNESLK 457
Cdd:pfam00068  81 SSCEKQLCECDKAAAECFARATYNKKYK 108
Phospholip_A2_1 pfam00068
Phospholipase A2; Phospholipase A2 releases fatty acids from the second carbon group of ...
 78-184 4.77e-34

Phospholipase A2; Phospholipase A2 releases fatty acids from the second carbon group of glycerol. Perhaps the best known members are secreted snake venoms, but also found in secreted pancreatic and membrane-associated forms. Structure is all-alpha, with two core disulfide-linked helices and a calcium-binding loop. This alignment represents the major family of PLA2s. A second minor family, defined by the honeybee venom PLA2 PDB:1POC and related sequences from Gila monsters (Heloderma), is not recognized. This minor family conserves the core helix pair but is substantially different elsewhere. The PROSITE pattern PA2_HIS, specific to the first core helix, recognizes both families.


Pssm-ID: 459659  Cd Length: 108  Bit Score: 124.26  E-value: 4.77e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024468187  78 LLNFVNKMKCVSG-FCPRDFEDYGCSCRFEMEGLPVDEADECCFQHRKCYEEAMEMECtWDPSKISTDVTCSAENLSCEN 156
Cdd:pfam00068   1 LWQFGEMIKCTTGrNPPLDYNDYGCYCGLGGSGTPVDATDRCCQAHDCCYERLKKLGC-GNPYLLSYNYSCSDGTITCSG 79

                          90       100
                  ....*....|....*....|....*...
gi 2024468187 157 GDPCEQFLCTCDKDAIECFGNAHINSSL 184
Cdd:pfam00068  80 NSSCEKQLCECDKAAAECFARATYNKKY 107
PA2c smart00085
Phospholipase A2;
353-454 1.69e-17

Phospholipase A2;


Pssm-ID: 214508  Cd Length: 117  Bit Score: 78.40  E-value: 1.69e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024468187  353 QLGEMLFCLTERCPE-EFESYGCYCGQEGRGHPTDALDRCCFSHHCCVEQVKTLGC--PAERSSRSevvCFDHMPKCIGW 429
Cdd:smart00085   4 QFGNMIQCATGKRAWlSYGDYGCYCGWGGSGTPVDATDRCCFVHDCCYGKAEKEGCnpKTTTYSYS---CDNGFITCGGK 80

                           90       100
                   ....*....|....*....|....*.
gi 2024468187  430 -SLCEKLLCACDQTAAQCMASALFNE 454
Cdd:smart00085  81 nTACLVFVCECDRAAAICFAKNPYNK 106
PA2c smart00085
Phospholipase A2;
78-181 3.38e-15

Phospholipase A2;


Pssm-ID: 214508  Cd Length: 117  Bit Score: 71.85  E-value: 3.38e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024468187   78 LLNFVNKMKCVSGFCP-RDFEDYGCSCRFEMEGLPVDEADECCFQHRKCYEEAMEMECtwDPSKISTDVTCSAENLSC-E 155
Cdd:smart00085   2 LWQFGNMIQCATGKRAwLSYGDYGCYCGWGGSGTPVDATDRCCFVHDCCYGKAEKEGC--NPKTTTYSYSCDNGFITCgG 79

                           90       100
                   ....*....|....*....|....*.
gi 2024468187  156 NGDPCEQFLCTCDKDAIECFGNAHIN 181
Cdd:smart00085  80 KNTACLVFVCECDRAAAICFAKNPYN 105
 
Name Accession Description Interval E-value
otoconin_90 cd04707
otoconin_90: Phospholipase A2-like domains present in otoconin-90 and otoconin-95, mammal ...
 353-469 2.83e-58

otoconin_90: Phospholipase A2-like domains present in otoconin-90 and otoconin-95, mammal proteins that are principal matrix proteins of calcitic otoconia. Interactions involving otoconin-90 may trigger or constitute key events in otoconia formation. The PLA2-like domains in otoconins may have lost their metal-binding sites.


Pssm-ID: 153096  Cd Length: 117  Bit Score: 189.22  E-value: 2.83e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024468187 353 QLGEMLFCLTERCPEEFESYGCYCGQEGRGHPTDALDRCCFSHHCCVEQVKTLGCPAERSSRSEVVCFDHMPKCIGWSLC 432
Cdd:cd04707     1 QLGEMLKCLTGRCPREFEDYGCYCGQEGEGLPVDELDRCCFQHRCCLEQASEMGCLQDRKLSTEVTCVDHKPKCEGVSVC 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2024468187 433 EKLLCACDQTAAQCMASALFNESLKFPHGQVCQEEKA 469
Cdd:cd04707    81 EKLLCTCDKTAAECMAAAHFNSSLNSLDVSSCPGQVP 117
otoconin_90 cd04707
otoconin_90: Phospholipase A2-like domains present in otoconin-90 and otoconin-95, mammal ...
 80-197 1.98e-53

otoconin_90: Phospholipase A2-like domains present in otoconin-90 and otoconin-95, mammal proteins that are principal matrix proteins of calcitic otoconia. Interactions involving otoconin-90 may trigger or constitute key events in otoconia formation. The PLA2-like domains in otoconins may have lost their metal-binding sites.


Pssm-ID: 153096  Cd Length: 117  Bit Score: 176.51  E-value: 1.98e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024468187  80 NFVNKMKCVSGFCPRDFEDYGCSCRFEMEGLPVDEADECCFQHRKCYEEAMEMECTWDpSKISTDVTCSAENLSCENGDP 159
Cdd:cd04707     1 QLGEMLKCLTGRCPREFEDYGCYCGQEGEGLPVDELDRCCFQHRCCLEQASEMGCLQD-RKLSTEVTCVDHKPKCEGVSV 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2024468187 160 CEQFLCTCDKDAIECFGNAHINSSLNGLDVSSCPSLVT 197
Cdd:cd04707    80 CEKLLCTCDKTAAECMAAAHFNSSLNSLDVSSCPGQVP 117
Phospholip_A2_1 pfam00068
Phospholipase A2; Phospholipase A2 releases fatty acids from the second carbon group of ...
 351-457 1.36e-41

Phospholipase A2; Phospholipase A2 releases fatty acids from the second carbon group of glycerol. Perhaps the best known members are secreted snake venoms, but also found in secreted pancreatic and membrane-associated forms. Structure is all-alpha, with two core disulfide-linked helices and a calcium-binding loop. This alignment represents the major family of PLA2s. A second minor family, defined by the honeybee venom PLA2 PDB:1POC and related sequences from Gila monsters (Heloderma), is not recognized. This minor family conserves the core helix pair but is substantially different elsewhere. The PROSITE pattern PA2_HIS, specific to the first core helix, recognizes both families.


Pssm-ID: 459659  Cd Length: 108  Bit Score: 144.67  E-value: 1.36e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024468187 351 LPQLGEMLFCLTER-CPEEFESYGCYCGQEGRGHPTDALDRCCFSHHCCVEQVKTLGCPAERSSRSEVVCFDHMPKCIGW 429
Cdd:pfam00068   1 LWQFGEMIKCTTGRnPPLDYNDYGCYCGLGGSGTPVDATDRCCQAHDCCYERLKKLGCGNPYLLSYNYSCSDGTITCSGN 80

                          90       100
                  ....*....|....*....|....*...
gi 2024468187 430 SLCEKLLCACDQTAAQCMASALFNESLK 457
Cdd:pfam00068  81 SSCEKQLCECDKAAAECFARATYNKKYK 108
Phospholip_A2_1 pfam00068
Phospholipase A2; Phospholipase A2 releases fatty acids from the second carbon group of ...
 78-184 4.77e-34

Phospholipase A2; Phospholipase A2 releases fatty acids from the second carbon group of glycerol. Perhaps the best known members are secreted snake venoms, but also found in secreted pancreatic and membrane-associated forms. Structure is all-alpha, with two core disulfide-linked helices and a calcium-binding loop. This alignment represents the major family of PLA2s. A second minor family, defined by the honeybee venom PLA2 PDB:1POC and related sequences from Gila monsters (Heloderma), is not recognized. This minor family conserves the core helix pair but is substantially different elsewhere. The PROSITE pattern PA2_HIS, specific to the first core helix, recognizes both families.


Pssm-ID: 459659  Cd Length: 108  Bit Score: 124.26  E-value: 4.77e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024468187  78 LLNFVNKMKCVSG-FCPRDFEDYGCSCRFEMEGLPVDEADECCFQHRKCYEEAMEMECtWDPSKISTDVTCSAENLSCEN 156
Cdd:pfam00068   1 LWQFGEMIKCTTGrNPPLDYNDYGCYCGLGGSGTPVDATDRCCQAHDCCYERLKKLGC-GNPYLLSYNYSCSDGTITCSG 79

                          90       100
                  ....*....|....*....|....*...
gi 2024468187 157 GDPCEQFLCTCDKDAIECFGNAHINSSL 184
Cdd:pfam00068  80 NSSCEKQLCECDKAAAECFARATYNKKY 107
PLA2c cd00125
PLA2c: Phospholipase A2, a family of secretory and cytosolic enzymes; the latter are either Ca ...
 77-192 4.69e-24

PLA2c: Phospholipase A2, a family of secretory and cytosolic enzymes; the latter are either Ca dependent or Ca independent. PLA2 cleaves the sn-2 position of the glycerol backbone of phospholipids (PC or phosphatidylethanolamine), usually in a metal-dependent reaction, to generate lysophospholipid (LysoPL) and a free fatty acid (FA). The resulting products are either dietary or used in synthetic pathways for leukotrienes and prostaglandins. Often, arachidonic acid is released as a free fatty acid and acts as second messenger in signaling networks. Secreted PLA2s have also been found to specifically bind to a variety of soluble and membrane proteins in mammals, including receptors. As a toxin, PLA2 is a potent presynaptic neurotoxin which blocks nerve terminals by binding to the nerve membrane and hydrolyzing stable membrane lipids. The products of the hydrolysis (LysoPL and FA) cannot form bilayers leading to a change in membrane conformation and ultimately to a block in the release of neurotransmitters. PLA2 may form dimers or oligomers.


Pssm-ID: 153091  Cd Length: 115  Bit Score: 96.94  E-value: 4.69e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024468187  77 ALLNFVNKMKCVSGFCPRDFEDYGCSCRFEMEGLPVDEADECCFQHRKCYEEAMEMECtwDPSKISTDVTCSAENLSCEN 156
Cdd:cd00125     1 NLLQFGKMIKCTTGRSALDYNGYGCYCGLGGSGTPVDDTDRCCQVHDCCYDRAEKGGC--SPYFTSYSYTCSDGQITCSD 78

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2024468187 157 G-DPCEQFLCTCDKDAIECFGNAHINSSLNGLDVSSC 192
Cdd:cd00125    79 AnDKCARALCECDRAAALCFARAPYNPKYRNYDKKRC 115
PLA2c cd00125
PLA2c: Phospholipase A2, a family of secretory and cytosolic enzymes; the latter are either Ca ...
 353-464 5.89e-23

PLA2c: Phospholipase A2, a family of secretory and cytosolic enzymes; the latter are either Ca dependent or Ca independent. PLA2 cleaves the sn-2 position of the glycerol backbone of phospholipids (PC or phosphatidylethanolamine), usually in a metal-dependent reaction, to generate lysophospholipid (LysoPL) and a free fatty acid (FA). The resulting products are either dietary or used in synthetic pathways for leukotrienes and prostaglandins. Often, arachidonic acid is released as a free fatty acid and acts as second messenger in signaling networks. Secreted PLA2s have also been found to specifically bind to a variety of soluble and membrane proteins in mammals, including receptors. As a toxin, PLA2 is a potent presynaptic neurotoxin which blocks nerve terminals by binding to the nerve membrane and hydrolyzing stable membrane lipids. The products of the hydrolysis (LysoPL and FA) cannot form bilayers leading to a change in membrane conformation and ultimately to a block in the release of neurotransmitters. PLA2 may form dimers or oligomers.


Pssm-ID: 153091  Cd Length: 115  Bit Score: 93.85  E-value: 5.89e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024468187 353 QLGEMLFCLTERCPEEFESYGCYCGQEGRGHPTDALDRCCFSHHCCVEQVKTLGCPAE------RSSRSEVVCFDHMPKc 426
Cdd:cd00125     4 QFGKMIKCTTGRSALDYNGYGCYCGLGGSGTPVDDTDRCCQVHDCCYDRAEKGGCSPYftsysyTCSDGQITCSDANDK- 82

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2024468187 427 igwslCEKLLCACDQTAAQCMASALFNESLKFPHGQVC 464
Cdd:cd00125    83 -----CARALCECDRAAALCFARAPYNPKYRNYDKKRC 115
PLA2_like cd00618
PLA2_like: Phospholipase A2, a super-family of secretory and cytosolic enzymes; the latter are ...
 372-450 1.64e-17

PLA2_like: Phospholipase A2, a super-family of secretory and cytosolic enzymes; the latter are either Ca dependent or Ca independent. PLA2 cleaves the sn-2 position of the glycerol backbone of phospholipids (PC or phosphatidylethanolamine), usually in a metal-dependent reaction, to generate lysophospholipid (LysoPL) and a free fatty acid (FA). The resulting products are either dietary or used in synthetic pathways for leukotrienes and prostaglandins. Often, arachidonic acid is released as a free fatty acid and acts as second messenger in signaling networks. Secreted PLA2s have also been found to specifically bind to a variety of soluble and membrane proteins in mammals, including receptors. As a toxin, PLA2 is a potent presynaptic neurotoxin which blocks nerve terminals by binding to the nerve membrane and hydrolyzing stable membrane lipids. The products of the hydrolysis (LysoPL and FA) cannot form bilayers leading to a change in membrane conformation and ultimately to a block in the release of neurotransmitters. PLA2 may form dimers or oligomers.


Pssm-ID: 153092  Cd Length: 83  Bit Score: 77.22  E-value: 1.64e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024468187 372 YGCYCGQEGR----GHPTDALDRCCFSHHCCVEQVKTLGCPAERSSRSevVCFDHMPKCIGWSLCEKLLCACDQTAAQCM 447
Cdd:cd00618     3 YGCYCGPGGSacpsGQPVDETDRCCRKHDCCYDQISDGGCCDGCLSYS--FSEGGVTCLTNSDLCTRSHCDCDRRLAICL 80


                  ...
gi 2024468187 448 ASA 450
Cdd:cd00618    81 ARA 83
PA2c smart00085
Phospholipase A2;
353-454 1.69e-17

Phospholipase A2;


Pssm-ID: 214508  Cd Length: 117  Bit Score: 78.40  E-value: 1.69e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024468187  353 QLGEMLFCLTERCPE-EFESYGCYCGQEGRGHPTDALDRCCFSHHCCVEQVKTLGC--PAERSSRSevvCFDHMPKCIGW 429
Cdd:smart00085   4 QFGNMIQCATGKRAWlSYGDYGCYCGWGGSGTPVDATDRCCFVHDCCYGKAEKEGCnpKTTTYSYS---CDNGFITCGGK 80

                           90       100
                   ....*....|....*....|....*.
gi 2024468187  430 -SLCEKLLCACDQTAAQCMASALFNE 454
Cdd:smart00085  81 nTACLVFVCECDRAAAICFAKNPYNK 106
PLA2_like cd00618
PLA2_like: Phospholipase A2, a super-family of secretory and cytosolic enzymes; the latter are ...
 98-178 1.91e-15

PLA2_like: Phospholipase A2, a super-family of secretory and cytosolic enzymes; the latter are either Ca dependent or Ca independent. PLA2 cleaves the sn-2 position of the glycerol backbone of phospholipids (PC or phosphatidylethanolamine), usually in a metal-dependent reaction, to generate lysophospholipid (LysoPL) and a free fatty acid (FA). The resulting products are either dietary or used in synthetic pathways for leukotrienes and prostaglandins. Often, arachidonic acid is released as a free fatty acid and acts as second messenger in signaling networks. Secreted PLA2s have also been found to specifically bind to a variety of soluble and membrane proteins in mammals, including receptors. As a toxin, PLA2 is a potent presynaptic neurotoxin which blocks nerve terminals by binding to the nerve membrane and hydrolyzing stable membrane lipids. The products of the hydrolysis (LysoPL and FA) cannot form bilayers leading to a change in membrane conformation and ultimately to a block in the release of neurotransmitters. PLA2 may form dimers or oligomers.


Pssm-ID: 153092  Cd Length: 83  Bit Score: 71.44  E-value: 1.91e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024468187  98 DYGCSCRFEME----GLPVDEADECCFQHRKCYEEAMEMECTWDPSKIStdvTCSAENLSCENGDPCEQFLCTCDKDAIE 173
Cdd:cd00618     2 PYGCYCGPGGSacpsGQPVDETDRCCRKHDCCYDQISDGGCCDGCLSYS---FSEGGVTCLTNSDLCTRSHCDCDRRLAI 78


                  ....*
gi 2024468187 174 CFGNA 178
Cdd:cd00618    79 CLARA 83
PA2c smart00085
Phospholipase A2;
78-181 3.38e-15

Phospholipase A2;


Pssm-ID: 214508  Cd Length: 117  Bit Score: 71.85  E-value: 3.38e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024468187   78 LLNFVNKMKCVSGFCP-RDFEDYGCSCRFEMEGLPVDEADECCFQHRKCYEEAMEMECtwDPSKISTDVTCSAENLSC-E 155
Cdd:smart00085   2 LWQFGNMIQCATGKRAwLSYGDYGCYCGWGGSGTPVDATDRCCFVHDCCYGKAEKEGC--NPKTTTYSYSCDNGFITCgG 79

                           90       100
                   ....*....|....*....|....*.
gi 2024468187  156 NGDPCEQFLCTCDKDAIECFGNAHIN 181
Cdd:smart00085  80 KNTACLVFVCECDRAAAICFAKNPYN 105
 
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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