NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|57222994|gb|AAW41038|]
View 

expressed protein [Cryptococcus neoformans var. neoformans JEC21]

Protein Classification

phospholipase B family protein( domain architecture ID 10110727)

phospholipase B family protein is part of the SGNH-family of lipolytic enzymes that may have both esterase and phospholipase-A/lysophospholipase activity; it may be a membrane protein involved in the conversion of phosphatidylcholine to fatty acids and glycerophosphocholine

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
Phospholipase_B_like cd01824
Phospholipase-B_like. This subgroup of the SGNH-family of lipolytic enzymes may have both ...
60-391 3.55e-87

Phospholipase-B_like. This subgroup of the SGNH-family of lipolytic enzymes may have both esterase and phospholipase-A/lysophospholipase activity. It's members may be involved in the conversion of phosphatidylcholine to fatty acids and glycerophosphocholine, perhaps in the context of dietary lipid uptake. Members may be membrane proteins. The tertiary fold of the SGNH-hydrolases is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; Its active site closely resembles two of the three components of typical Ser-His-Asp(Glu) triad from other serine hydrolases.


:

Pssm-ID: 238862  Cd Length: 288  Bit Score: 266.90  E-value: 3.55e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57222994  60 AKDVRPDDFRVVMALGDSITAGLLARgsrsssassapsqvdpqrpLLPFLDI-QEYRGLSYPIGSDP---GAITIPEILR 135
Cdd:cd01824   2 VHRLRPGDIKVIAALGDSLTAGNGAG-------------------SANNLDLlTEYRGLSWSIGGDStlrGLTTLPNILR 62
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57222994 136 HFSPSAKEIPGSSKGkhppvtclngwgikgcaERPEEDGLNAAVSGSVSSGLLRQVEDFILPRLKDMEI-RKEDWKFVNL 214
Cdd:cd01824  63 EFNPSLYGYSVGTGD-----------------ETLPDSGFNVAEPGAKSEDLPQQARLLVRRMKKDPRVdFKNDWKLITI 125
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57222994 215 GIGANDICSFCLYSNMtdidfnGSPKRFAKDIKRAVNALRKNVPNIIINIIGLFRVSAIYKLTLKDPYCQPPLFPYpiph 294
Cdd:cd01824 126 FIGGNDLCSLCEDANP------GSPQTFVKNLRKALDILRDEVPRAFVNLVGLLNVASLRSLTKKPLQCETLLAPE---- 195
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57222994 295 fplgCSCALLPGPTGDwtrQKMDELGEAYDEAVLEIVREWEKeDDEHFGAIWQPGTAID----LPNYPITALSPIDCFHP 370
Cdd:cd01824 196 ----CPCLLGPTENSY---QDLKKFYKEYQNEVEEIVESGEF-DREDFAVVVQPFFEDTslppLPDGPDLSFFSPDCFHF 267
                       330       340
                ....*....|....*....|.
gi 57222994 371 SEASHQRMAAGIWNRLTLSLE 391
Cdd:cd01824 268 SQRGHAIAANALWNNLLEPVG 288
 
Name Accession Description Interval E-value
Phospholipase_B_like cd01824
Phospholipase-B_like. This subgroup of the SGNH-family of lipolytic enzymes may have both ...
60-391 3.55e-87

Phospholipase-B_like. This subgroup of the SGNH-family of lipolytic enzymes may have both esterase and phospholipase-A/lysophospholipase activity. It's members may be involved in the conversion of phosphatidylcholine to fatty acids and glycerophosphocholine, perhaps in the context of dietary lipid uptake. Members may be membrane proteins. The tertiary fold of the SGNH-hydrolases is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; Its active site closely resembles two of the three components of typical Ser-His-Asp(Glu) triad from other serine hydrolases.


Pssm-ID: 238862  Cd Length: 288  Bit Score: 266.90  E-value: 3.55e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57222994  60 AKDVRPDDFRVVMALGDSITAGLLARgsrsssassapsqvdpqrpLLPFLDI-QEYRGLSYPIGSDP---GAITIPEILR 135
Cdd:cd01824   2 VHRLRPGDIKVIAALGDSLTAGNGAG-------------------SANNLDLlTEYRGLSWSIGGDStlrGLTTLPNILR 62
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57222994 136 HFSPSAKEIPGSSKGkhppvtclngwgikgcaERPEEDGLNAAVSGSVSSGLLRQVEDFILPRLKDMEI-RKEDWKFVNL 214
Cdd:cd01824  63 EFNPSLYGYSVGTGD-----------------ETLPDSGFNVAEPGAKSEDLPQQARLLVRRMKKDPRVdFKNDWKLITI 125
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57222994 215 GIGANDICSFCLYSNMtdidfnGSPKRFAKDIKRAVNALRKNVPNIIINIIGLFRVSAIYKLTLKDPYCQPPLFPYpiph 294
Cdd:cd01824 126 FIGGNDLCSLCEDANP------GSPQTFVKNLRKALDILRDEVPRAFVNLVGLLNVASLRSLTKKPLQCETLLAPE---- 195
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57222994 295 fplgCSCALLPGPTGDwtrQKMDELGEAYDEAVLEIVREWEKeDDEHFGAIWQPGTAID----LPNYPITALSPIDCFHP 370
Cdd:cd01824 196 ----CPCLLGPTENSY---QDLKKFYKEYQNEVEEIVESGEF-DREDFAVVVQPFFEDTslppLPDGPDLSFFSPDCFHF 267
                       330       340
                ....*....|....*....|.
gi 57222994 371 SEASHQRMAAGIWNRLTLSLE 391
Cdd:cd01824 268 SQRGHAIAANALWNNLLEPVG 288
Lipase_GDSL pfam00657
GDSL-like Lipase/Acylhydrolase;
174-382 1.42e-14

GDSL-like Lipase/Acylhydrolase;


Pssm-ID: 459892 [Multi-domain]  Cd Length: 210  Bit Score: 72.22  E-value: 1.42e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57222994   174 GLNAAVSGSVSSGLLRQVEDFilPRLKDMEIRKEDWKFVNLGIGANDICSFClysnmtdidfnGSPKRFAKDIKRAVNAL 253
Cdd:pfam00657  44 GANFAIGGATIEDLPIQLEQL--LRLISDVKDQAKPDLVTIFIGANDLCNFL-----------SSPARSKKRVPDLLDEL 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57222994   254 RKNVPnIIINIIGLFRVSAIYkltlkdpycqpplfpypiphfPLGCscallpgPTGDWTRQKMDELGEAYDEAVLEIVRE 333
Cdd:pfam00657 111 RANLP-QLGLGARKFWVHGLG---------------------PLGC-------TPPKGCYELYNALAEEYNERLNELVNS 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 57222994   334 WEKEDDEhFGAIWQPGTAIDLPNYPITAL-SPIDCFHPSEASHQRMAAGI 382
Cdd:pfam00657 162 LAAAAED-ANVVYVDIYGFEDPTDPCCGIgLEPDGLHPSEKGYKAVAEAI 210
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
175-386 7.91e-06

Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle control, cell division, chromosome partitioning, Lipid transport and metabolism];


Pssm-ID: 442045 [Multi-domain]  Cd Length: 191  Bit Score: 46.18  E-value: 7.91e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57222994 175 LNAAVSGSVSSGLLRQVEDfilprlkdmEIRKEDWKFVNLGIGANDICSfclysnmtdiDFNGSPKRFAKDIKRAVNALR 254
Cdd:COG2755  46 VNAGISGATTADLLARLDR---------DLLALKPDLVVIELGTNDLLR----------GLGVSPEEFRANLEALIDRLR 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57222994 255 KNVPNIiiniiglfrvsaiykltlkDPYCQpplfpypiphfplgcscallpGPTGDWTRQKMDELGEAYDEAVLEIVREw 334
Cdd:COG2755 107 AAGPGA-------------------RVVLV---------------------TPPPRLRPNYLNERIEAYNAAIRELAAE- 145
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 57222994 335 ekeddehFGAIWQPGTAIDLPNYPITALSPIDCFHPSEASHQRMAAGIWNRL 386
Cdd:COG2755 146 -------YGVPLVDLYAALRDAGDLPDLLTADGLHPNAAGYRLIAEAVLPAL 190
 
Name Accession Description Interval E-value
Phospholipase_B_like cd01824
Phospholipase-B_like. This subgroup of the SGNH-family of lipolytic enzymes may have both ...
60-391 3.55e-87

Phospholipase-B_like. This subgroup of the SGNH-family of lipolytic enzymes may have both esterase and phospholipase-A/lysophospholipase activity. It's members may be involved in the conversion of phosphatidylcholine to fatty acids and glycerophosphocholine, perhaps in the context of dietary lipid uptake. Members may be membrane proteins. The tertiary fold of the SGNH-hydrolases is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; Its active site closely resembles two of the three components of typical Ser-His-Asp(Glu) triad from other serine hydrolases.


Pssm-ID: 238862  Cd Length: 288  Bit Score: 266.90  E-value: 3.55e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57222994  60 AKDVRPDDFRVVMALGDSITAGLLARgsrsssassapsqvdpqrpLLPFLDI-QEYRGLSYPIGSDP---GAITIPEILR 135
Cdd:cd01824   2 VHRLRPGDIKVIAALGDSLTAGNGAG-------------------SANNLDLlTEYRGLSWSIGGDStlrGLTTLPNILR 62
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57222994 136 HFSPSAKEIPGSSKGkhppvtclngwgikgcaERPEEDGLNAAVSGSVSSGLLRQVEDFILPRLKDMEI-RKEDWKFVNL 214
Cdd:cd01824  63 EFNPSLYGYSVGTGD-----------------ETLPDSGFNVAEPGAKSEDLPQQARLLVRRMKKDPRVdFKNDWKLITI 125
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57222994 215 GIGANDICSFCLYSNMtdidfnGSPKRFAKDIKRAVNALRKNVPNIIINIIGLFRVSAIYKLTLKDPYCQPPLFPYpiph 294
Cdd:cd01824 126 FIGGNDLCSLCEDANP------GSPQTFVKNLRKALDILRDEVPRAFVNLVGLLNVASLRSLTKKPLQCETLLAPE---- 195
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57222994 295 fplgCSCALLPGPTGDwtrQKMDELGEAYDEAVLEIVREWEKeDDEHFGAIWQPGTAID----LPNYPITALSPIDCFHP 370
Cdd:cd01824 196 ----CPCLLGPTENSY---QDLKKFYKEYQNEVEEIVESGEF-DREDFAVVVQPFFEDTslppLPDGPDLSFFSPDCFHF 267
                       330       340
                ....*....|....*....|.
gi 57222994 371 SEASHQRMAAGIWNRLTLSLE 391
Cdd:cd01824 268 SQRGHAIAANALWNNLLEPVG 288
Lipase_GDSL pfam00657
GDSL-like Lipase/Acylhydrolase;
174-382 1.42e-14

GDSL-like Lipase/Acylhydrolase;


Pssm-ID: 459892 [Multi-domain]  Cd Length: 210  Bit Score: 72.22  E-value: 1.42e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57222994   174 GLNAAVSGSVSSGLLRQVEDFilPRLKDMEIRKEDWKFVNLGIGANDICSFClysnmtdidfnGSPKRFAKDIKRAVNAL 253
Cdd:pfam00657  44 GANFAIGGATIEDLPIQLEQL--LRLISDVKDQAKPDLVTIFIGANDLCNFL-----------SSPARSKKRVPDLLDEL 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57222994   254 RKNVPnIIINIIGLFRVSAIYkltlkdpycqpplfpypiphfPLGCscallpgPTGDWTRQKMDELGEAYDEAVLEIVRE 333
Cdd:pfam00657 111 RANLP-QLGLGARKFWVHGLG---------------------PLGC-------TPPKGCYELYNALAEEYNERLNELVNS 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 57222994   334 WEKEDDEhFGAIWQPGTAIDLPNYPITAL-SPIDCFHPSEASHQRMAAGI 382
Cdd:pfam00657 162 LAAAAED-ANVVYVDIYGFEDPTDPCCGIgLEPDGLHPSEKGYKAVAEAI 210
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
175-386 7.91e-06

Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle control, cell division, chromosome partitioning, Lipid transport and metabolism];


Pssm-ID: 442045 [Multi-domain]  Cd Length: 191  Bit Score: 46.18  E-value: 7.91e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57222994 175 LNAAVSGSVSSGLLRQVEDfilprlkdmEIRKEDWKFVNLGIGANDICSfclysnmtdiDFNGSPKRFAKDIKRAVNALR 254
Cdd:COG2755  46 VNAGISGATTADLLARLDR---------DLLALKPDLVVIELGTNDLLR----------GLGVSPEEFRANLEALIDRLR 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57222994 255 KNVPNIiiniiglfrvsaiykltlkDPYCQpplfpypiphfplgcscallpGPTGDWTRQKMDELGEAYDEAVLEIVREw 334
Cdd:COG2755 107 AAGPGA-------------------RVVLV---------------------TPPPRLRPNYLNERIEAYNAAIRELAAE- 145
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 57222994 335 ekeddehFGAIWQPGTAIDLPNYPITALSPIDCFHPSEASHQRMAAGIWNRL 386
Cdd:COG2755 146 -------YGVPLVDLYAALRDAGDLPDLLTADGLHPNAAGYRLIAEAVLPAL 190
FeeA_FeeB_like cd01836
SGNH_hydrolase subfamily, FeeA, FeeB and similar esterases/lipases. FeeA and FeeB are part of ...
177-382 3.82e-05

SGNH_hydrolase subfamily, FeeA, FeeB and similar esterases/lipases. FeeA and FeeB are part of a biosynthetic gene cluster and may participate in the biosynthesis of long-chain N-acyltyrosines by providing saturated and unsaturated fatty acids, which it turn are loaded onto the acyl carrier protein FeeL. SGNH hydrolases are a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases.


Pssm-ID: 238874  Cd Length: 191  Bit Score: 44.18  E-value: 3.82e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57222994 177 AAVSGSVSSGLLRQVEdfilprlkdmEIRKEDWKFVNLGIGANDIcsfclySNMTdidfngSPKRFAKDIKRAVNALRKN 256
Cdd:cd01836  46 FAKTGATSADLLRQLA----------PLPETRFDVAVISIGVNDV------THLT------SIARWRKQLAELVDALRAK 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57222994 257 vpniiiniiglFRVSAIYKLTLkdpycqPPLFPYPiphfplgcscaLLPGPTGDWTRQKMDELGEAYDEAVLEivrewek 336
Cdd:cd01836 104 -----------FPGARVVVTAV------PPLGRFP-----------ALPQPLRWLLGRRARLLNRALERLASE------- 148
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 57222994 337 eddehfgaiWQPGTAIDLPNYPITALSPIDCFHPSEASHQRMAAGI 382
Cdd:cd01836 149 ---------APRVTLLPATGPLFPALFASDGFHPSAAGYAVWAEAL 185
SGNH_hydrolase cd00229
SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary ...
176-384 1.34e-04

SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the typical Ser-His-Asp(Glu) triad from other serine hydrolases, but may lack the carboxlic acid.


Pssm-ID: 238141 [Multi-domain]  Cd Length: 187  Bit Score: 42.78  E-value: 1.34e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57222994 176 NAAVSGSVSSGLLRQVEDFILprlkdmeIRKEDWKFVNLGIGANDICSFCLYsnmtdidfngSPKRFAKDIKRAVNALRK 255
Cdd:cd00229  40 NLGVSGATTADALRRLGLRLA-------LLKDKPDLVIIELGTNDLGRGGDT----------SIDEFKANLEELLDALRE 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57222994 256 NVPniiiniiglfrvsaiykltlkdpycqpplfpypiphfplGCSCALLPGPTGDWTRQKMDELGEAYDEAVLEIVREWE 335
Cdd:cd00229 103 RAP---------------------------------------GAKVILITPPPPPPREGLLGRALPRYNEAIKAVAAENP 143
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 57222994 336 KEDDEHFGAIWQPGTAIDLPNYpitalsPIDCFHPSEASHQRMAAGIWN 384
Cdd:cd00229 144 APSGVDLVDLAALLGDEDKSLY------SPDGIHPNPAGHKLIAEALAS 186
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH