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Conserved domains on  [gi|1907187815|ref|XP_036009728|]
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phospholipase A2 group XV isoform X1 [Mus musculus]

Protein Classification

alpha/beta hydrolase family protein( domain architecture ID 229394)

alpha/beta hydrolase family protein may catalyze the hydrolysis of substrates with different chemical composition or physicochemical properties using a nucleophile-His-acid catalytic triad

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Abhydrolase super family cl21494
alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, ...
45-357 3.13e-93

alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, peroxidases, esterases, epoxide hydrolases and dehalogenases. The catalytic apparatus typically involves three residues (catalytic triad): a serine, a glutamate or aspartate and a histidine, and often the mechanism involves a nucleophilic attack on a carbonyl carbon atom.


The actual alignment was detected with superfamily member pfam02450:

Pssm-ID: 473884  Cd Length: 383  Bit Score: 284.06  E-value: 3.13e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187815  45 PVIIDCWIDNIRLVYNRTSRATQFPDGVDVRVP-GFgetFSMEFLDPSKRNVGSYFYTMVESLVGWGYTRGEDVRGAPYD 123
Cdd:pfam02450  11 PLVVDCWIDNTHVVLNPSTGLQPDPPGVKIRAAqGF---ESVEYLDYSKLAGYWIWHKVVQNLVNIGYERNKTVRAAPYD 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187815 124 WRRAPNENGPYFLALREMIEEMYQMYGGPVVLVAHSMGNVYMLYFLQR-QPQVWKDKYIHAFVSLGAPWGGVAKTLRVLA 202
Cdd:pfam02450  88 WRLSLEERDKYFHKLKQLIEEAHKLYGKKVVLIGHSMGNLLVLYFLLWvVAEAWKDQHIDAFISLGAPLLGSPKAVRALA 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187815 203 SGDNNRIPVIGPLKIREQQRSAVSTSWLLPY-------NHTWSHEKVFVYTPTTNYTLRDYHRFFRD-----------IG 264
Cdd:pfam02450 168 SGYNFGIPILSEITLRGLQRSFSSSPWMLPKgkyvlwsDVAWPSDEIFIQTPSINYTYGALVRFFDDetinvdalgftLN 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187815 265 FEDGWFMRQDTEGL------------------------VEAMTPPGVELHCLYGTGVPTPNSFYYES-----------FP 309
Cdd:pfam02450 248 TLDGWYMWKVSRDLdgglpyleaelakndikywvnpeeTPLPVAPGVKVYCIYGVGLPTERGYYYTPgktsspilsriDY 327
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907187815 310 DRDPKICFGDGDGTVNLESVLQCQAWQS-RQEHRVSLQELP----GSEHIEML 357
Cdd:pfam02450 328 EDPVGIVSGDGDGTVPKRSLELCKNWQGlPAGQNVTVHELKhgsrSAEHVDIL 380
 
Name Accession Description Interval E-value
LCAT pfam02450
Lecithin:cholesterol acyltransferase; Lecithin:cholesterol acyltransferase (LCAT) is involved ...
45-357 3.13e-93

Lecithin:cholesterol acyltransferase; Lecithin:cholesterol acyltransferase (LCAT) is involved in extracellular metabolism of plasma lipoproteins, including cholesterol.


Pssm-ID: 396835  Cd Length: 383  Bit Score: 284.06  E-value: 3.13e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187815  45 PVIIDCWIDNIRLVYNRTSRATQFPDGVDVRVP-GFgetFSMEFLDPSKRNVGSYFYTMVESLVGWGYTRGEDVRGAPYD 123
Cdd:pfam02450  11 PLVVDCWIDNTHVVLNPSTGLQPDPPGVKIRAAqGF---ESVEYLDYSKLAGYWIWHKVVQNLVNIGYERNKTVRAAPYD 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187815 124 WRRAPNENGPYFLALREMIEEMYQMYGGPVVLVAHSMGNVYMLYFLQR-QPQVWKDKYIHAFVSLGAPWGGVAKTLRVLA 202
Cdd:pfam02450  88 WRLSLEERDKYFHKLKQLIEEAHKLYGKKVVLIGHSMGNLLVLYFLLWvVAEAWKDQHIDAFISLGAPLLGSPKAVRALA 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187815 203 SGDNNRIPVIGPLKIREQQRSAVSTSWLLPY-------NHTWSHEKVFVYTPTTNYTLRDYHRFFRD-----------IG 264
Cdd:pfam02450 168 SGYNFGIPILSEITLRGLQRSFSSSPWMLPKgkyvlwsDVAWPSDEIFIQTPSINYTYGALVRFFDDetinvdalgftLN 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187815 265 FEDGWFMRQDTEGL------------------------VEAMTPPGVELHCLYGTGVPTPNSFYYES-----------FP 309
Cdd:pfam02450 248 TLDGWYMWKVSRDLdgglpyleaelakndikywvnpeeTPLPVAPGVKVYCIYGVGLPTERGYYYTPgktsspilsriDY 327
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907187815 310 DRDPKICFGDGDGTVNLESVLQCQAWQS-RQEHRVSLQELP----GSEHIEML 357
Cdd:pfam02450 328 EDPVGIVSGDGDGTVPKRSLELCKNWQGlPAGQNVTVHELKhgsrSAEHVDIL 380
PLN02733 PLN02733
phosphatidylcholine-sterol O-acyltransferase
83-193 3.67e-13

phosphatidylcholine-sterol O-acyltransferase


Pssm-ID: 215390  Cd Length: 440  Bit Score: 70.43  E-value: 3.67e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187815  83 FSMEFLDPS---KRNVGSYFYTMVESLVGWGYTRGEDVRGAPYDWRRApNENGPYFLALREMIEEMYQMYGGPVV-LVAH 158
Cdd:PLN02733   91 YAIDILDPDviiRLDEVYYFHDMIEQLIKWGYKEGKTLFGFGYDFRQS-NRLPETMDGLKKKLETVYKASGGKKVnIISH 169
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1907187815 159 SMGNVYMLYFLQRQPQVWkDKYIHAFVSLGAPWGG 193
Cdd:PLN02733  170 SMGGLLVKCFMSLHSDVF-EKYVNSWIAIAAPFQG 203
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
76-191 8.15e-09

Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and metabolism];


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 52.91  E-value: 8.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187815  76 VPGFGETfsmefldpskrnvGSYFYTMVESLVGWGYTrgedVRGAPYDWRRAPNENgpYFLALREMIEEMYQMYG-GPVV 154
Cdd:COG1075    11 VHGLGGS-------------AASWAPLAPRLRAAGYP----VYALNYPSTNGSIED--SAEQLAAFVDAVLAATGaEKVD 71
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1907187815 155 LVAHSMGNVYMLYFLQRQPqvwKDKYIHAFVSLGAPW 191
Cdd:COG1075    72 LVGHSMGGLVARYYLKRLG---GAAKVARVVTLGTPH 105
 
Name Accession Description Interval E-value
LCAT pfam02450
Lecithin:cholesterol acyltransferase; Lecithin:cholesterol acyltransferase (LCAT) is involved ...
45-357 3.13e-93

Lecithin:cholesterol acyltransferase; Lecithin:cholesterol acyltransferase (LCAT) is involved in extracellular metabolism of plasma lipoproteins, including cholesterol.


Pssm-ID: 396835  Cd Length: 383  Bit Score: 284.06  E-value: 3.13e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187815  45 PVIIDCWIDNIRLVYNRTSRATQFPDGVDVRVP-GFgetFSMEFLDPSKRNVGSYFYTMVESLVGWGYTRGEDVRGAPYD 123
Cdd:pfam02450  11 PLVVDCWIDNTHVVLNPSTGLQPDPPGVKIRAAqGF---ESVEYLDYSKLAGYWIWHKVVQNLVNIGYERNKTVRAAPYD 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187815 124 WRRAPNENGPYFLALREMIEEMYQMYGGPVVLVAHSMGNVYMLYFLQR-QPQVWKDKYIHAFVSLGAPWGGVAKTLRVLA 202
Cdd:pfam02450  88 WRLSLEERDKYFHKLKQLIEEAHKLYGKKVVLIGHSMGNLLVLYFLLWvVAEAWKDQHIDAFISLGAPLLGSPKAVRALA 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187815 203 SGDNNRIPVIGPLKIREQQRSAVSTSWLLPY-------NHTWSHEKVFVYTPTTNYTLRDYHRFFRD-----------IG 264
Cdd:pfam02450 168 SGYNFGIPILSEITLRGLQRSFSSSPWMLPKgkyvlwsDVAWPSDEIFIQTPSINYTYGALVRFFDDetinvdalgftLN 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187815 265 FEDGWFMRQDTEGL------------------------VEAMTPPGVELHCLYGTGVPTPNSFYYES-----------FP 309
Cdd:pfam02450 248 TLDGWYMWKVSRDLdgglpyleaelakndikywvnpeeTPLPVAPGVKVYCIYGVGLPTERGYYYTPgktsspilsriDY 327
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907187815 310 DRDPKICFGDGDGTVNLESVLQCQAWQS-RQEHRVSLQELP----GSEHIEML 357
Cdd:pfam02450 328 EDPVGIVSGDGDGTVPKRSLELCKNWQGlPAGQNVTVHELKhgsrSAEHVDIL 380
PLN02733 PLN02733
phosphatidylcholine-sterol O-acyltransferase
83-193 3.67e-13

phosphatidylcholine-sterol O-acyltransferase


Pssm-ID: 215390  Cd Length: 440  Bit Score: 70.43  E-value: 3.67e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187815  83 FSMEFLDPS---KRNVGSYFYTMVESLVGWGYTRGEDVRGAPYDWRRApNENGPYFLALREMIEEMYQMYGGPVV-LVAH 158
Cdd:PLN02733   91 YAIDILDPDviiRLDEVYYFHDMIEQLIKWGYKEGKTLFGFGYDFRQS-NRLPETMDGLKKKLETVYKASGGKKVnIISH 169
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1907187815 159 SMGNVYMLYFLQRQPQVWkDKYIHAFVSLGAPWGG 193
Cdd:PLN02733  170 SMGGLLVKCFMSLHSDVF-EKYVNSWIAIAAPFQG 203
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
76-191 8.15e-09

Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and metabolism];


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 52.91  E-value: 8.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187815  76 VPGFGETfsmefldpskrnvGSYFYTMVESLVGWGYTrgedVRGAPYDWRRAPNENgpYFLALREMIEEMYQMYG-GPVV 154
Cdd:COG1075    11 VHGLGGS-------------AASWAPLAPRLRAAGYP----VYALNYPSTNGSIED--SAEQLAAFVDAVLAATGaEKVD 71
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1907187815 155 LVAHSMGNVYMLYFLQRQPqvwKDKYIHAFVSLGAPW 191
Cdd:COG1075    72 LVGHSMGGLVARYYLKRLG---GAAKVARVVTLGTPH 105
PLN02517 PLN02517
phosphatidylcholine-sterol O-acyltransferase
50-212 1.17e-06

phosphatidylcholine-sterol O-acyltransferase


Pssm-ID: 178132  Cd Length: 642  Bit Score: 50.53  E-value: 1.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187815  50 CWIDNIRLvYNRTSRAtqfPDGVDVR-VPGFgetFSMEFLDPSkrnvgsYFY--TMVESLVGWGYtRGEDVRGAPYDWRR 126
Cdd:PLN02517  119 CWVEHMSL-DNETGLD---PPGIRVRaVSGL---VAADYFAPG------YFVwaVLIANLARIGY-EEKNMYMAAYDWRL 184
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187815 127 APNENGPYFLALREM---IEEMYQMYGG-PVVLVAHSMGNVYMLYFLQ--RQPQV--------WKDKYIHAFVSLGAPWG 192
Cdd:PLN02517  185 SFQNTEVRDQTLSRLksnIELMVATNGGkKVVVVPHSMGVLYFLHFMKwvEAPAPmgggggpgWCAKHIKAVMNIGGPFL 264
                         170       180
                  ....*....|....*....|
gi 1907187815 193 GVAKTLRVLASGDNNRIPVI 212
Cdd:PLN02517  265 GVPKAVSGLFSAEAKDIAVA 284
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
53-174 2.56e-04

Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 41.91  E-value: 2.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187815  53 DNIRLVYnRTSRATQFPDGVDVRVPGFGETfsmefldpskrnvGSYFYTMVESLVGWGYT------RG----EDVRGAPY 122
Cdd:COG2267    12 DGLRLRG-RRWRPAGSPRGTVVLVHGLGEH-------------SGRYAELAEALAAAGYAvlafdlRGhgrsDGPRGHVD 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907187815 123 DWRRapnengpYFLALREMIEEMYQMYGGPVVLVAHSMGNVYMLYFLQRQPQ 174
Cdd:COG2267    78 SFDD-------YVDDLRAALDALRARPGLPVVLLGHSMGGLIALLYAARYPD 122
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
69-209 5.99e-04

Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is approximately 110 amino acids in length. It is found in association with pfam00561. The majority of the members in this family carry the exopeptidase active-site residues of Ser-122, Asp-239 and His-269 as in UniProtKB:Q7ZWC2.


Pssm-ID: 463473 [Multi-domain]  Cd Length: 238  Bit Score: 41.05  E-value: 5.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187815  69 PDGVDVRVPGFGETfsmefldpskrnVGSYFYTmVESLVGWGYtrgeDVRGapYDWR---RAPNENGP-----YFLA-LR 139
Cdd:pfam12146   3 PRAVVVLVHGLGEH------------SGRYAHL-ADALAAQGF----AVYA--YDHRghgRSDGKRGHvpsfdDYVDdLD 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187815 140 EMIEEMYQMYGG-PVVLVAHSMGNVYMLYFLQRQPQVW------------KDKYIHAFVSLGAPWGG-VAKTLRVLASGD 205
Cdd:pfam12146  64 TFVDKIREEHPGlPLFLLGHSMGGLIAALYALRYPDKVdglilsapalkiKPYLAPPILKLLAKLLGkLFPRLRVPNNLL 143

                  ....
gi 1907187815 206 NNRI 209
Cdd:pfam12146 144 PDSL 147
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
116-248 1.62e-03

alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.


Pssm-ID: 395444 [Multi-domain]  Cd Length: 245  Bit Score: 39.80  E-value: 1.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187815 116 DVRGAPYDwRRAPNENGPYFLALREMIEEMYQMYG-GPVVLVAHSMGNVYMLYFLQRQPQvwkdkYIHAFVSLGAPwggv 194
Cdd:pfam00561  34 DLRGFGKS-SRPKAQDDYRTDDLAEDLEYILEALGlEKVNLVGHSMGGLIALAYAAKYPD-----RVKALVLLGAL---- 103
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907187815 195 aktLRVLASGDNNRIPVIGPLKIREQQRSAVSTSWLLPYnhtWSHEKVFVYTPT 248
Cdd:pfam00561 104 ---DPPHELDEADRFILALFPGFFDGFVADFAPNPLGRL---VAKLLALLLLRL 151
 
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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