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Conserved domains on  [gi|767945353|ref|XP_011513636|]
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acyloxyacyl hydrolase isoform X2 [Homo sapiens]

Protein Classification

SapB and acyloxyacyl_hydrolase_like domain-containing protein( domain architecture ID 12219227)

protein containing domains SapB, Cu-binding_MopE, and acyloxyacyl_hydrolase_like

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
acyloxyacyl_hydrolase_like cd01826
Acyloxyacyl-hydrolase like subfamily of the SGNH-hydrolase family. Acyloxyacyl-hydrolase is a ...
 212-511 0e+00

Acyloxyacyl-hydrolase like subfamily of the SGNH-hydrolase family. Acyloxyacyl-hydrolase is a leukocyte-secreted enzyme that deacetylates bacterial lipopolysaccharides.


:

Pssm-ID: 238864  Cd Length: 305  Bit Score: 540.85  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945353 212 YEKKFCEGSQPRGIILLGDSAGAHFHISPEWITASQMSLNSFINLPTALTNELDWPQLSGATGFLDST---VGIKEKSIY 288
Cdd:cd01826    1 YEELLCGNSQPMGVILLGDSAGAHFHIPPEWLTVLLLSSEGFANIITIIANEFDWPMLSGATGFANSTryiIGGFTDSLY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945353 289 LRLWKRNHCNHRDYQNISRNGASSRNLKKFIESLSRNKVLDYPAIVIYAMIGNDVCSGKSDPvPAMTTPEKLYSNVMQTL 368
Cdd:cd01826   81 LRLRERNRCNHRDYQNLGVNGASSRNLLSIIKSIARNRTTDKPALVIYSMIGNDVCNGPNDT-INHTTPEEFYENVMEAL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945353 369 KHLNSHLPNGSHVILYGLPDGTFLWDNLHNRYHPLGQLNKDMTYAQLYSFLNCLQVSPCHGWMSSNKTLRTLTSERAEQL 448
Cdd:cd01826  160 KYLDTKLPNGSHVILVGLVDGRILYDTLHNRLHPIGQLNKDVTYPNLYDYLNCLQVSPCWGWLNSNETLRNLTSERAAQL 239

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767945353 449 SNTLKKIAASEKFTNFNLFYMDFAFHEIIQEWQKRGGQPWQLIEPVDGFHPNERKSILLKGIL 511
Cdd:cd01826  240 SNVLKRIAANETFNNFDVHYIDFPIQQIVDMWIAFGGQTWQLIEPVDGFHPSQIANALLAEVF 302
SapB smart00741
Saposin (B) Domains; Present in multiple copies in prosaposin and in pulmonary ...
 45-82 8.11e-06

Saposin (B) Domains; Present in multiple copies in prosaposin and in pulmonary surfactant-associated protein B. In plant aspartic proteinases, a saposin domain is circularly permuted. This causes the prediction algorithm to predict two such domains, where only one is truly present.


:

Pssm-ID: 214797 [Multi-domain]  Cd Length: 76  Bit Score: 44.02  E-value: 8.11e-06
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 767945353    45 LFLKTTCYLVIDKFGSDIIKLLSADMNADVVCHTLEFC 82
Cdd:smart00741  39 KSLSDQCKEFVDQYGPEIIDLLEQGLDPKDVCQKLGLC 76
Cu-binding_MopE pfam11617
Putative metal-binding motif; The seqeunce of structure 2vov is not matched in any other ...
 173-201 4.74e-04

Putative metal-binding motif; The seqeunce of structure 2vov is not matched in any other sequence either in UniProt or in NCBI (Sep2014). The model is of a short repeat not found on the G1UBC6 - 2vov - protein. The presence of conserved cysteine residues and the lack of hydrophobic residues suggests that this repeat might be a metal-binding site, perhaps for zinc or calcium ions.


:

Pssm-ID: 463309 [Multi-domain]  Cd Length: 28  Bit Score: 37.86  E-value: 4.74e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 767945353  173 DCNDSDESVYPGR--RPNNwdvhQDSNCNGI 201
Cdd:pfam11617   1 DCDDSDPAIHPGAaeICDG----IDNNCDGV 27
 
Name Accession Description Interval E-value
acyloxyacyl_hydrolase_like cd01826
Acyloxyacyl-hydrolase like subfamily of the SGNH-hydrolase family. Acyloxyacyl-hydrolase is a ...
 212-511 0e+00

Acyloxyacyl-hydrolase like subfamily of the SGNH-hydrolase family. Acyloxyacyl-hydrolase is a leukocyte-secreted enzyme that deacetylates bacterial lipopolysaccharides.


Pssm-ID: 238864  Cd Length: 305  Bit Score: 540.85  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945353 212 YEKKFCEGSQPRGIILLGDSAGAHFHISPEWITASQMSLNSFINLPTALTNELDWPQLSGATGFLDST---VGIKEKSIY 288
Cdd:cd01826    1 YEELLCGNSQPMGVILLGDSAGAHFHIPPEWLTVLLLSSEGFANIITIIANEFDWPMLSGATGFANSTryiIGGFTDSLY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945353 289 LRLWKRNHCNHRDYQNISRNGASSRNLKKFIESLSRNKVLDYPAIVIYAMIGNDVCSGKSDPvPAMTTPEKLYSNVMQTL 368
Cdd:cd01826   81 LRLRERNRCNHRDYQNLGVNGASSRNLLSIIKSIARNRTTDKPALVIYSMIGNDVCNGPNDT-INHTTPEEFYENVMEAL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945353 369 KHLNSHLPNGSHVILYGLPDGTFLWDNLHNRYHPLGQLNKDMTYAQLYSFLNCLQVSPCHGWMSSNKTLRTLTSERAEQL 448
Cdd:cd01826  160 KYLDTKLPNGSHVILVGLVDGRILYDTLHNRLHPIGQLNKDVTYPNLYDYLNCLQVSPCWGWLNSNETLRNLTSERAAQL 239

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767945353 449 SNTLKKIAASEKFTNFNLFYMDFAFHEIIQEWQKRGGQPWQLIEPVDGFHPNERKSILLKGIL 511
Cdd:cd01826  240 SNVLKRIAANETFNNFDVHYIDFPIQQIVDMWIAFGGQTWQLIEPVDGFHPSQIANALLAEVF 302
Lipase_GDSL pfam00657
GDSL-like Lipase/Acylhydrolase;
225-501 7.34e-16

GDSL-like Lipase/Acylhydrolase;


Pssm-ID: 459892 [Multi-domain]  Cd Length: 210  Bit Score: 76.84  E-value: 7.34e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945353  225 IILLGDSAGAHFHISPewitasqmslnsfinlptalTNELDWPQLSGAtgFLDSTVGIKEKSIylrlwkrnhcnhRDYQN 304
Cdd:pfam00657   1 IVAFGDSLTDGGGDGP--------------------GGRFSWGDLLAD--FLARKLGVPGSGY------------NHGAN 46

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945353  305 ISRNGASSRN----LKKFIESLSRNKVLDYPAIVIYAMIGNDVCSGKSDPvpamttpEKLYSNVMQTLKHLNSHLPN--- 377
Cdd:pfam00657  47 FAIGGATIEDlpiqLEQLLRLISDVKDQAKPDLVTIFIGANDLCNFLSSP-------ARSKKRVPDLLDELRANLPQlgl 119

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945353  378 -GSHVILYGLPdgtflwdnlhnryhPLGQLnkdmtyaqlysflnclqvsPCHGWMssnKTLRTLTSERAEQLSNTLKKIA 456
Cdd:pfam00657 120 gARKFWVHGLG--------------PLGCT-------------------PPKGCY---ELYNALAEEYNERLNELVNSLA 163

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 767945353  457 AseKFTNFNLFYMDFA-FHEIIQEWQKRGGQPwqliepvDGFHPNE 501
Cdd:pfam00657 164 A--AAEDANVVYVDIYgFEDPTDPCCGIGLEP-------DGLHPSE 200
SapB smart00741
Saposin (B) Domains; Present in multiple copies in prosaposin and in pulmonary ...
 45-82 8.11e-06

Saposin (B) Domains; Present in multiple copies in prosaposin and in pulmonary surfactant-associated protein B. In plant aspartic proteinases, a saposin domain is circularly permuted. This causes the prediction algorithm to predict two such domains, where only one is truly present.


Pssm-ID: 214797 [Multi-domain]  Cd Length: 76  Bit Score: 44.02  E-value: 8.11e-06
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 767945353    45 LFLKTTCYLVIDKFGSDIIKLLSADMNADVVCHTLEFC 82
Cdd:smart00741  39 KSLSDQCKEFVDQYGPEIIDLLEQGLDPKDVCQKLGLC 76
SapB_2 pfam03489
Saposin-like type B, region 2; Saposin B is a small non-enzymatic glycoprotein required for ...
 49-82 8.21e-06

Saposin-like type B, region 2; Saposin B is a small non-enzymatic glycoprotein required for the breakdown of cerebroside sulphates (sulphatides) in lysosomes. Saposin B contains three intramolecular disulphide bridges, exists as a dimer and is remarkably heat, protease and pH stable. The crystal structure of human saposin B reveals an unusual shell-like dimer consisting of a monolayer of alpha-helices enclosing a large hydrophobic cavity. It is one of the most studied members of the saposin protein family and it is involved in the hydrolysis of glycolipids and glycerolipids. SapB is unique in the saposin family in that it facilitates degradation by interacting with the substrate, not the enzymes.


Pssm-ID: 460945  Cd Length: 34  Bit Score: 42.95  E-value: 8.21e-06
                          10        20        30
                  ....*....|....*....|....*....|....
gi 767945353   49 TTCYLVIDKFGSDIIKLLSADMNADVVCHTLEFC 82
Cdd:pfam03489   1 DECKSLVDQYGPLIIDLLESELDPKDVCTALGLC 34
Cu-binding_MopE pfam11617
Putative metal-binding motif; The seqeunce of structure 2vov is not matched in any other ...
 173-201 4.74e-04

Putative metal-binding motif; The seqeunce of structure 2vov is not matched in any other sequence either in UniProt or in NCBI (Sep2014). The model is of a short repeat not found on the G1UBC6 - 2vov - protein. The presence of conserved cysteine residues and the lack of hydrophobic residues suggests that this repeat might be a metal-binding site, perhaps for zinc or calcium ions.


Pssm-ID: 463309 [Multi-domain]  Cd Length: 28  Bit Score: 37.86  E-value: 4.74e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 767945353  173 DCNDSDESVYPGR--RPNNwdvhQDSNCNGI 201
Cdd:pfam11617   1 DCDDSDPAIHPGAaeICDG----IDNNCDGV 27
 
Name Accession Description Interval E-value
acyloxyacyl_hydrolase_like cd01826
Acyloxyacyl-hydrolase like subfamily of the SGNH-hydrolase family. Acyloxyacyl-hydrolase is a ...
 212-511 0e+00

Acyloxyacyl-hydrolase like subfamily of the SGNH-hydrolase family. Acyloxyacyl-hydrolase is a leukocyte-secreted enzyme that deacetylates bacterial lipopolysaccharides.


Pssm-ID: 238864  Cd Length: 305  Bit Score: 540.85  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945353 212 YEKKFCEGSQPRGIILLGDSAGAHFHISPEWITASQMSLNSFINLPTALTNELDWPQLSGATGFLDST---VGIKEKSIY 288
Cdd:cd01826    1 YEELLCGNSQPMGVILLGDSAGAHFHIPPEWLTVLLLSSEGFANIITIIANEFDWPMLSGATGFANSTryiIGGFTDSLY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945353 289 LRLWKRNHCNHRDYQNISRNGASSRNLKKFIESLSRNKVLDYPAIVIYAMIGNDVCSGKSDPvPAMTTPEKLYSNVMQTL 368
Cdd:cd01826   81 LRLRERNRCNHRDYQNLGVNGASSRNLLSIIKSIARNRTTDKPALVIYSMIGNDVCNGPNDT-INHTTPEEFYENVMEAL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945353 369 KHLNSHLPNGSHVILYGLPDGTFLWDNLHNRYHPLGQLNKDMTYAQLYSFLNCLQVSPCHGWMSSNKTLRTLTSERAEQL 448
Cdd:cd01826  160 KYLDTKLPNGSHVILVGLVDGRILYDTLHNRLHPIGQLNKDVTYPNLYDYLNCLQVSPCWGWLNSNETLRNLTSERAAQL 239

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767945353 449 SNTLKKIAASEKFTNFNLFYMDFAFHEIIQEWQKRGGQPWQLIEPVDGFHPNERKSILLKGIL 511
Cdd:cd01826  240 SNVLKRIAANETFNNFDVHYIDFPIQQIVDMWIAFGGQTWQLIEPVDGFHPSQIANALLAEVF 302
Lipase_GDSL pfam00657
GDSL-like Lipase/Acylhydrolase;
225-501 7.34e-16

GDSL-like Lipase/Acylhydrolase;


Pssm-ID: 459892 [Multi-domain]  Cd Length: 210  Bit Score: 76.84  E-value: 7.34e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945353  225 IILLGDSAGAHFHISPewitasqmslnsfinlptalTNELDWPQLSGAtgFLDSTVGIKEKSIylrlwkrnhcnhRDYQN 304
Cdd:pfam00657   1 IVAFGDSLTDGGGDGP--------------------GGRFSWGDLLAD--FLARKLGVPGSGY------------NHGAN 46

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945353  305 ISRNGASSRN----LKKFIESLSRNKVLDYPAIVIYAMIGNDVCSGKSDPvpamttpEKLYSNVMQTLKHLNSHLPN--- 377
Cdd:pfam00657  47 FAIGGATIEDlpiqLEQLLRLISDVKDQAKPDLVTIFIGANDLCNFLSSP-------ARSKKRVPDLLDELRANLPQlgl 119

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945353  378 -GSHVILYGLPdgtflwdnlhnryhPLGQLnkdmtyaqlysflnclqvsPCHGWMssnKTLRTLTSERAEQLSNTLKKIA 456
Cdd:pfam00657 120 gARKFWVHGLG--------------PLGCT-------------------PPKGCY---ELYNALAEEYNERLNELVNSLA 163

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 767945353  457 AseKFTNFNLFYMDFA-FHEIIQEWQKRGGQPwqliepvDGFHPNE 501
Cdd:pfam00657 164 A--AAEDANVVYVDIYgFEDPTDPCCGIGLEP-------DGLHPSE 200
SapB smart00741
Saposin (B) Domains; Present in multiple copies in prosaposin and in pulmonary ...
 45-82 8.11e-06

Saposin (B) Domains; Present in multiple copies in prosaposin and in pulmonary surfactant-associated protein B. In plant aspartic proteinases, a saposin domain is circularly permuted. This causes the prediction algorithm to predict two such domains, where only one is truly present.


Pssm-ID: 214797 [Multi-domain]  Cd Length: 76  Bit Score: 44.02  E-value: 8.11e-06
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 767945353    45 LFLKTTCYLVIDKFGSDIIKLLSADMNADVVCHTLEFC 82
Cdd:smart00741  39 KSLSDQCKEFVDQYGPEIIDLLEQGLDPKDVCQKLGLC 76
SapB_2 pfam03489
Saposin-like type B, region 2; Saposin B is a small non-enzymatic glycoprotein required for ...
 49-82 8.21e-06

Saposin-like type B, region 2; Saposin B is a small non-enzymatic glycoprotein required for the breakdown of cerebroside sulphates (sulphatides) in lysosomes. Saposin B contains three intramolecular disulphide bridges, exists as a dimer and is remarkably heat, protease and pH stable. The crystal structure of human saposin B reveals an unusual shell-like dimer consisting of a monolayer of alpha-helices enclosing a large hydrophobic cavity. It is one of the most studied members of the saposin protein family and it is involved in the hydrolysis of glycolipids and glycerolipids. SapB is unique in the saposin family in that it facilitates degradation by interacting with the substrate, not the enzymes.


Pssm-ID: 460945  Cd Length: 34  Bit Score: 42.95  E-value: 8.21e-06
                          10        20        30
                  ....*....|....*....|....*....|....
gi 767945353   49 TTCYLVIDKFGSDIIKLLSADMNADVVCHTLEFC 82
Cdd:pfam03489   1 DECKSLVDQYGPLIIDLLESELDPKDVCTALGLC 34
Cu-binding_MopE pfam11617
Putative metal-binding motif; The seqeunce of structure 2vov is not matched in any other ...
 173-201 4.74e-04

Putative metal-binding motif; The seqeunce of structure 2vov is not matched in any other sequence either in UniProt or in NCBI (Sep2014). The model is of a short repeat not found on the G1UBC6 - 2vov - protein. The presence of conserved cysteine residues and the lack of hydrophobic residues suggests that this repeat might be a metal-binding site, perhaps for zinc or calcium ions.


Pssm-ID: 463309 [Multi-domain]  Cd Length: 28  Bit Score: 37.86  E-value: 4.74e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 767945353  173 DCNDSDESVYPGR--RPNNwdvhQDSNCNGI 201
Cdd:pfam11617   1 DCDDSDPAIHPGAaeICDG----IDNNCDGV 27
SGNH_hydrolase cd00229
SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary ...
 286-400 2.79e-03

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: 39.32  E-value: 2.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767945353 286 SIYLRLWKRNHCNHRDYQNISRNGASSRNLKKFIESLSRnKVLDYPAIVIYAMIGNDVCSGksdpvpAMTTPEKLYSNVM 365
Cdd:cd00229   22 SLLLYLLLLAGGPGVEVINLGVSGATTADALRRLGLRLA-LLKDKPDLVIIELGTNDLGRG------GDTSIDEFKANLE 94

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 767945353 366 QTLKHLNSHLPnGSHVILYGLPDGTFLWDNLHNRY 400
Cdd:cd00229   95 ELLDALRERAP-GAKVILITPPPPPPREGLLGRAL 128
 
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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