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Conserved domains on  [gi|1039743758|ref|XP_017171010|]
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acyloxyacyl hydrolase isoform X2 [Mus musculus]

Protein Classification

putative metal-binding motif-containing protein( domain architecture ID 12219228)

putative metal-binding motif-containing protein similar to the N-terminal region of Methylococcus capsulatus-secreted protein MopE

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SGNH_hydrolase super family cl01053
SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary ...
 243-513 3.78e-161

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.


The actual alignment was detected with superfamily member cd01826:

Pssm-ID: 470049  Cd Length: 305  Bit Score: 462.65  E-value: 3.78e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743758 243 YEKKFCEGSQPRGIILLGDSAGAHFHIPPEWLTASQMSVNSFLNLPSALTDELNWPQLSGVTGFLDST---SGIEEKSIY 319
Cdd:cd01826     1 YEELLCGNSQPMGVILLGDSAGAHFHIPPEWLTVLLLSSEGFANIITIIANEFDWPMLSGATGFANSTryiIGGFTDSLY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743758 320 HRLRKRNHCNHRDYQSISKNGASSRNLKNFIESLSRNQASDHPAIVLYAMIGNDVCNSKADTVPeMTTPEQMYANVMQTL 399
Cdd:cd01826    81 LRLRERNRCNHRDYQNLGVNGASSRNLLSIIKSIARNRTTDKPALVIYSMIGNDVCNGPNDTIN-HTTPEEFYENVMEAL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743758 400 THLNSHLPNGSHVILYGLPDGTFLWDSLHNRYHPLGQLNKDVTYAQFFSFLRCLQ--------------------RAEQL 459
Cdd:cd01826   160 KYLDTKLPNGSHVILVGLVDGRILYDTLHNRLHPIGQLNKDVTYPNLYDYLNCLQvspcwgwlnsnetlrnltseRAAQL 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039743758 460 SNTLKKIATTETFANFDLFYVDFAFHEIIEDWQKRGGQPWQLIEPVDGFHPNEV 513
Cdd:cd01826   240 SNVLKRIAANETFNNFDVHYIDFPIQQIVDMWIAFGGQTWQLIEPVDGFHPSQI 293
SapB smart00741
Saposin (B) Domains; Present in multiple copies in prosaposin and in pulmonary ...
 39-113 1.96e-12

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: 62.89  E-value: 1.96e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039743758   39 SCLGCVVLVSVIEQLAEVHNSSVQV--AMERLCSYLPekLFLKTACYFLVQTFGSDIIKLLDEAMKADVVCYALEFC 113
Cdd:smart00741   2 LCELCEFVVKQLENLLKDNKTEEEIkkALEKVCKKLP--KSLSDQCKEFVDQYGPEIIDLLEQGLDPKDVCQKLGLC 76
Cu-binding_MopE pfam11617
Putative metal-binding motif; The seqeunce of structure 2vov is not matched in any other ...
 204-232 1.28e-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: 39.40  E-value: 1.28e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1039743758 204 DCNDSDKTVYPGR--RPDNwdihQDSNCNGI 232
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 ...
 243-513 3.78e-161

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: 462.65  E-value: 3.78e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743758 243 YEKKFCEGSQPRGIILLGDSAGAHFHIPPEWLTASQMSVNSFLNLPSALTDELNWPQLSGVTGFLDST---SGIEEKSIY 319
Cdd:cd01826     1 YEELLCGNSQPMGVILLGDSAGAHFHIPPEWLTVLLLSSEGFANIITIIANEFDWPMLSGATGFANSTryiIGGFTDSLY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743758 320 HRLRKRNHCNHRDYQSISKNGASSRNLKNFIESLSRNQASDHPAIVLYAMIGNDVCNSKADTVPeMTTPEQMYANVMQTL 399
Cdd:cd01826    81 LRLRERNRCNHRDYQNLGVNGASSRNLLSIIKSIARNRTTDKPALVIYSMIGNDVCNGPNDTIN-HTTPEEFYENVMEAL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743758 400 THLNSHLPNGSHVILYGLPDGTFLWDSLHNRYHPLGQLNKDVTYAQFFSFLRCLQ--------------------RAEQL 459
Cdd:cd01826   160 KYLDTKLPNGSHVILVGLVDGRILYDTLHNRLHPIGQLNKDVTYPNLYDYLNCLQvspcwgwlnsnetlrnltseRAAQL 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039743758 460 SNTLKKIATTETFANFDLFYVDFAFHEIIEDWQKRGGQPWQLIEPVDGFHPNEV 513
Cdd:cd01826   240 SNVLKRIAANETFNNFDVHYIDFPIQQIVDMWIAFGGQTWQLIEPVDGFHPSQI 293
Lipase_GDSL pfam00657
GDSL-like Lipase/Acylhydrolase;
331-514 5.52e-15

GDSL-like Lipase/Acylhydrolase;


Pssm-ID: 459892 [Multi-domain]  Cd Length: 210  Bit Score: 74.15  E-value: 5.52e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743758 331 RDYQSISKNGASSRN----LKNFIESLSRNQASDHPAIVLYAMIGNDVCNSKADtvpemttPEQMYANVMQTLTHLNSHL 406
Cdd:pfam00657  42 NHGANFAIGGATIEDlpiqLEQLLRLISDVKDQAKPDLVTIFIGANDLCNFLSS-------PARSKKRVPDLLDELRANL 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743758 407 PN----GSHVILYGLPD-GTFLWDSLHNRYHPLGQlnkdvtyaqffsflrclQRAEQLSNTLKKIAttETFANFDLFYVD 481
Cdd:pfam00657 115 PQlglgARKFWVHGLGPlGCTPPKGCYELYNALAE-----------------EYNERLNELVNSLA--AAAEDANVVYVD 175

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1039743758 482 FA-FHEIIEDWQKRGGQPwqliepvDGFHPNEVG 514
Cdd:pfam00657 176 IYgFEDPTDPCCGIGLEP-------DGLHPSEKG 202
SapB smart00741
Saposin (B) Domains; Present in multiple copies in prosaposin and in pulmonary ...
 39-113 1.96e-12

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: 62.89  E-value: 1.96e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039743758   39 SCLGCVVLVSVIEQLAEVHNSSVQV--AMERLCSYLPekLFLKTACYFLVQTFGSDIIKLLDEAMKADVVCYALEFC 113
Cdd:smart00741   2 LCELCEFVVKQLENLLKDNKTEEEIkkALEKVCKKLP--KSLSDQCKEFVDQYGPEIIDLLEQGLDPKDVCQKLGLC 76
Cu-binding_MopE pfam11617
Putative metal-binding motif; The seqeunce of structure 2vov is not matched in any other ...
 204-232 1.28e-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: 39.40  E-value: 1.28e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1039743758 204 DCNDSDKTVYPGR--RPDNwdihQDSNCNGI 232
Cdd:pfam11617   1 DCDDSDPAIHPGAaeICDG----IDNNCDGV 27
SapB_2 pfam03489
Saposin-like type B, region 2; Saposin B is a small non-enzymatic glycoprotein required for ...
 82-113 3.71e-04

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: 37.94  E-value: 3.71e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1039743758  82 CYFLVQTFGSDIIKLLDEAMKADVVCYALEFC 113
Cdd:pfam03489   3 CKSLVDQYGPLIIDLLESELDPKDVCTALGLC 34
 
Name Accession Description Interval E-value
acyloxyacyl_hydrolase_like cd01826
Acyloxyacyl-hydrolase like subfamily of the SGNH-hydrolase family. Acyloxyacyl-hydrolase is a ...
 243-513 3.78e-161

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: 462.65  E-value: 3.78e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743758 243 YEKKFCEGSQPRGIILLGDSAGAHFHIPPEWLTASQMSVNSFLNLPSALTDELNWPQLSGVTGFLDST---SGIEEKSIY 319
Cdd:cd01826     1 YEELLCGNSQPMGVILLGDSAGAHFHIPPEWLTVLLLSSEGFANIITIIANEFDWPMLSGATGFANSTryiIGGFTDSLY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743758 320 HRLRKRNHCNHRDYQSISKNGASSRNLKNFIESLSRNQASDHPAIVLYAMIGNDVCNSKADTVPeMTTPEQMYANVMQTL 399
Cdd:cd01826    81 LRLRERNRCNHRDYQNLGVNGASSRNLLSIIKSIARNRTTDKPALVIYSMIGNDVCNGPNDTIN-HTTPEEFYENVMEAL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743758 400 THLNSHLPNGSHVILYGLPDGTFLWDSLHNRYHPLGQLNKDVTYAQFFSFLRCLQ--------------------RAEQL 459
Cdd:cd01826   160 KYLDTKLPNGSHVILVGLVDGRILYDTLHNRLHPIGQLNKDVTYPNLYDYLNCLQvspcwgwlnsnetlrnltseRAAQL 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039743758 460 SNTLKKIATTETFANFDLFYVDFAFHEIIEDWQKRGGQPWQLIEPVDGFHPNEV 513
Cdd:cd01826   240 SNVLKRIAANETFNNFDVHYIDFPIQQIVDMWIAFGGQTWQLIEPVDGFHPSQI 293
Lipase_GDSL pfam00657
GDSL-like Lipase/Acylhydrolase;
331-514 5.52e-15

GDSL-like Lipase/Acylhydrolase;


Pssm-ID: 459892 [Multi-domain]  Cd Length: 210  Bit Score: 74.15  E-value: 5.52e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743758 331 RDYQSISKNGASSRN----LKNFIESLSRNQASDHPAIVLYAMIGNDVCNSKADtvpemttPEQMYANVMQTLTHLNSHL 406
Cdd:pfam00657  42 NHGANFAIGGATIEDlpiqLEQLLRLISDVKDQAKPDLVTIFIGANDLCNFLSS-------PARSKKRVPDLLDELRANL 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743758 407 PN----GSHVILYGLPD-GTFLWDSLHNRYHPLGQlnkdvtyaqffsflrclQRAEQLSNTLKKIAttETFANFDLFYVD 481
Cdd:pfam00657 115 PQlglgARKFWVHGLGPlGCTPPKGCYELYNALAE-----------------EYNERLNELVNSLA--AAAEDANVVYVD 175

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1039743758 482 FA-FHEIIEDWQKRGGQPwqliepvDGFHPNEVG 514
Cdd:pfam00657 176 IYgFEDPTDPCCGIGLEP-------DGLHPSEKG 202
SapB smart00741
Saposin (B) Domains; Present in multiple copies in prosaposin and in pulmonary ...
 39-113 1.96e-12

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: 62.89  E-value: 1.96e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039743758   39 SCLGCVVLVSVIEQLAEVHNSSVQV--AMERLCSYLPekLFLKTACYFLVQTFGSDIIKLLDEAMKADVVCYALEFC 113
Cdd:smart00741   2 LCELCEFVVKQLENLLKDNKTEEEIkkALEKVCKKLP--KSLSDQCKEFVDQYGPEIIDLLEQGLDPKDVCQKLGLC 76
SGNH_hydrolase cd00229
SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary ...
 308-527 6.12e-05

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: 44.33  E-value: 6.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743758 308 DSTSGIEEKSIYHRLRKRNHCNHRDYQSISKNGASSRNLKNFIESLSRNqASDHPAIVLYAMIGNDVCNSKAdtvpemTT 387
Cdd:cd00229    13 GASSGSTFYSLLLYLLLLAGGPGVEVINLGVSGATTADALRRLGLRLAL-LKDKPDLVIIELGTNDLGRGGD------TS 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743758 388 PEQMYANVMQTLTHLNSHLPnGSHVILYGLPDGTFLWDSLHNRYhplgqlnkdvtyaqffsflrclqraEQLSNTLKKIA 467
Cdd:cd00229    86 IDEFKANLEELLDALRERAP-GAKVILITPPPPPPREGLLGRAL-------------------------PRYNEAIKAVA 139

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743758 468 TTETFAnFDLFYVDFAFHEIIEDWQKRGgqpwqliepVDGFHPNEVGSgthvIVMGEQLA 527
Cdd:cd00229   140 AENPAP-SGVDLVDLAALLGDEDKSLYS---------PDGIHPNPAGH----KLIAEALA 185
Cu-binding_MopE pfam11617
Putative metal-binding motif; The seqeunce of structure 2vov is not matched in any other ...
 204-232 1.28e-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: 39.40  E-value: 1.28e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1039743758 204 DCNDSDKTVYPGR--RPDNwdihQDSNCNGI 232
Cdd:pfam11617   1 DCDDSDPAIHPGAaeICDG----IDNNCDGV 27
SapB_2 pfam03489
Saposin-like type B, region 2; Saposin B is a small non-enzymatic glycoprotein required for ...
 82-113 3.71e-04

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: 37.94  E-value: 3.71e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1039743758  82 CYFLVQTFGSDIIKLLDEAMKADVVCYALEFC 113
Cdd:pfam03489   3 CKSLVDQYGPLIIDLLESELDPKDVCTALGLC 34
 
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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