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Conserved domains on  [gi|2462613988|ref|XP_054214018|]
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acyloxyacyl hydrolase isoform X1 [Homo sapiens]

Protein Classification

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

putative metal-binding motif-containing protein similar to the N-terminal region of Methylococcus capsulatus-secreted protein MopE| saposin domain-containing protein such as saposins, which are accessory proteins that aid in the degradation of sphingolipids by hydrolytic enzymes

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 ...
244-518 4.56e-166

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: 477.29  E-value: 4.56e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613988 244 YEKKFCEGSQPRGIILLGDSAGAHFHISPEWITASQMSLNSFINLPTALTNELDWPQLSGATGFLDST---VGIKEKSIY 320
Cdd:cd01826     1 YEELLCGNSQPMGVILLGDSAGAHFHIPPEWLTVLLLSSEGFANIITIIANEFDWPMLSGATGFANSTryiIGGFTDSLY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613988 321 LRLWKRNHCNHRDYQNISRNGASSRNLKKFIE-----RKSD-PV------------------PAMTTPEKLYSNVMQTLK 376
Cdd:cd01826    81 LRLRERNRCNHRDYQNLGVNGASSRNLLSIIKsiarnRTTDkPAlviysmigndvcngpndtINHTTPEEFYENVMEALK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613988 377 HLNSHLPNGSHVILYGLPDGTFLWDNLHNRYHPLGQLNKDMTYAQLYSFLNCLQVSPCHGWMSSNKTLRTLTSERAEQLS 456
Cdd:cd01826   161 YLDTKLPNGSHVILVGLVDGRILYDTLHNRLHPIGQLNKDVTYPNLYDYLNCLQVSPCWGWLNSNETLRNLTSERAAQLS 240
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462613988 457 NTLKKIAASEKFTNFNLFYMDFAFHEIIQEWQKRGGQPWQLIEPVDGFHPNERKSILLKGIL 518
Cdd:cd01826   241 NVLKRIAANETFNNFDVHYIDFPIQQIVDMWIAFGGQTWQLIEPVDGFHPSQIANALLAEVF 302
SapB smart00741
Saposin (B) Domains; Present in multiple copies in prosaposin and in pulmonary ...
40-114 2.88e-13

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: 65.21  E-value: 2.88e-13
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462613988   40 TCVGCVLVVSVIEQLAQVHNS--TVQASMERLCSYLPekLFLKTTCYLVIDKFGSDIIKLLSADMNADVVCHTLEFC 114
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 ...
205-233 3.43e-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: 38.25  E-value: 3.43e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2462613988 205 DCNDSDESVYPGR--RPNNwdvhQDSNCNGI 233
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 ...
244-518 4.56e-166

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: 477.29  E-value: 4.56e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613988 244 YEKKFCEGSQPRGIILLGDSAGAHFHISPEWITASQMSLNSFINLPTALTNELDWPQLSGATGFLDST---VGIKEKSIY 320
Cdd:cd01826     1 YEELLCGNSQPMGVILLGDSAGAHFHIPPEWLTVLLLSSEGFANIITIIANEFDWPMLSGATGFANSTryiIGGFTDSLY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613988 321 LRLWKRNHCNHRDYQNISRNGASSRNLKKFIE-----RKSD-PV------------------PAMTTPEKLYSNVMQTLK 376
Cdd:cd01826    81 LRLRERNRCNHRDYQNLGVNGASSRNLLSIIKsiarnRTTDkPAlviysmigndvcngpndtINHTTPEEFYENVMEALK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613988 377 HLNSHLPNGSHVILYGLPDGTFLWDNLHNRYHPLGQLNKDMTYAQLYSFLNCLQVSPCHGWMSSNKTLRTLTSERAEQLS 456
Cdd:cd01826   161 YLDTKLPNGSHVILVGLVDGRILYDTLHNRLHPIGQLNKDVTYPNLYDYLNCLQVSPCWGWLNSNETLRNLTSERAAQLS 240
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462613988 457 NTLKKIAASEKFTNFNLFYMDFAFHEIIQEWQKRGGQPWQLIEPVDGFHPNERKSILLKGIL 518
Cdd:cd01826   241 NVLKRIAANETFNNFDVHYIDFPIQQIVDMWIAFGGQTWQLIEPVDGFHPSQIANALLAEVF 302
SapB smart00741
Saposin (B) Domains; Present in multiple copies in prosaposin and in pulmonary ...
40-114 2.88e-13

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: 65.21  E-value: 2.88e-13
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462613988   40 TCVGCVLVVSVIEQLAQVHNS--TVQASMERLCSYLPekLFLKTTCYLVIDKFGSDIIKLLSADMNADVVCHTLEFC 114
Cdd:smart00741   2 LCELCEFVVKQLENLLKDNKTeeEIKKALEKVCKKLP--KSLSDQCKEFVDQYGPEIIDLLEQGLDPKDVCQKLGLC 76
Lipase_GDSL pfam00657
GDSL-like Lipase/Acylhydrolase;
257-508 1.64e-07

GDSL-like Lipase/Acylhydrolase;


Pssm-ID: 459892 [Multi-domain]  Cd Length: 210  Bit Score: 52.19  E-value: 1.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613988 257 IILLGDSAGAHFHISPewitasqmslnsfinlptalTNELDWPQLSGAtgFLDSTVGIKEKSIylrlwkrnhcnhRDYQN 336
Cdd:pfam00657   1 IVAFGDSLTDGGGDGP--------------------GGRFSWGDLLAD--FLARKLGVPGSGY------------NHGAN 46
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613988 337 ISRNGASSRN----LKKFIERKSD----PVPAMTT--------------PEKLYSNVMQTLKHLNSHLPN----GSHVIL 390
Cdd:pfam00657  47 FAIGGATIEDlpiqLEQLLRLISDvkdqAKPDLVTifigandlcnflssPARSKKRVPDLLDELRANLPQlglgARKFWV 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613988 391 YGLPdgtflwdnlhnryhPLGQLnkdmtyaqlysflnclqvsPCHGWMssnKTLRTLTSERAEQLSNTLKKIAAseKFTN 470
Cdd:pfam00657 127 HGLG--------------PLGCT-------------------PPKGCY---ELYNALAEEYNERLNELVNSLAA--AAED 168
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 2462613988 471 FNLFYMDFA-FHEIIQEWQKRGGQPwqliepvDGFHPNE 508
Cdd:pfam00657 169 ANVVYVDIYgFEDPTDPCCGIGLEP-------DGLHPSE 200
SapB_2 pfam03489
Saposin-like type B, region 2; Saposin B is a small non-enzymatic glycoprotein required for ...
81-114 9.90e-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: 42.56  E-value: 9.90e-06
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2462613988  81 TTCYLVIDKFGSDIIKLLSADMNADVVCHTLEFC 114
Cdd:pfam03489   1 DECKSLVDQYGPLIIDLLESELDPKDVCTALGLC 34
Cu-binding_MopE pfam11617
Putative metal-binding motif; The seqeunce of structure 2vov is not matched in any other ...
205-233 3.43e-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: 38.25  E-value: 3.43e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2462613988 205 DCNDSDESVYPGR--RPNNwdvhQDSNCNGI 233
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 ...
244-518 4.56e-166

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: 477.29  E-value: 4.56e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613988 244 YEKKFCEGSQPRGIILLGDSAGAHFHISPEWITASQMSLNSFINLPTALTNELDWPQLSGATGFLDST---VGIKEKSIY 320
Cdd:cd01826     1 YEELLCGNSQPMGVILLGDSAGAHFHIPPEWLTVLLLSSEGFANIITIIANEFDWPMLSGATGFANSTryiIGGFTDSLY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613988 321 LRLWKRNHCNHRDYQNISRNGASSRNLKKFIE-----RKSD-PV------------------PAMTTPEKLYSNVMQTLK 376
Cdd:cd01826    81 LRLRERNRCNHRDYQNLGVNGASSRNLLSIIKsiarnRTTDkPAlviysmigndvcngpndtINHTTPEEFYENVMEALK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613988 377 HLNSHLPNGSHVILYGLPDGTFLWDNLHNRYHPLGQLNKDMTYAQLYSFLNCLQVSPCHGWMSSNKTLRTLTSERAEQLS 456
Cdd:cd01826   161 YLDTKLPNGSHVILVGLVDGRILYDTLHNRLHPIGQLNKDVTYPNLYDYLNCLQVSPCWGWLNSNETLRNLTSERAAQLS 240
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462613988 457 NTLKKIAASEKFTNFNLFYMDFAFHEIIQEWQKRGGQPWQLIEPVDGFHPNERKSILLKGIL 518
Cdd:cd01826   241 NVLKRIAANETFNNFDVHYIDFPIQQIVDMWIAFGGQTWQLIEPVDGFHPSQIANALLAEVF 302
SapB smart00741
Saposin (B) Domains; Present in multiple copies in prosaposin and in pulmonary ...
40-114 2.88e-13

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: 65.21  E-value: 2.88e-13
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462613988   40 TCVGCVLVVSVIEQLAQVHNS--TVQASMERLCSYLPekLFLKTTCYLVIDKFGSDIIKLLSADMNADVVCHTLEFC 114
Cdd:smart00741   2 LCELCEFVVKQLENLLKDNKTeeEIKKALEKVCKKLP--KSLSDQCKEFVDQYGPEIIDLLEQGLDPKDVCQKLGLC 76
Lipase_GDSL pfam00657
GDSL-like Lipase/Acylhydrolase;
257-508 1.64e-07

GDSL-like Lipase/Acylhydrolase;


Pssm-ID: 459892 [Multi-domain]  Cd Length: 210  Bit Score: 52.19  E-value: 1.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613988 257 IILLGDSAGAHFHISPewitasqmslnsfinlptalTNELDWPQLSGAtgFLDSTVGIKEKSIylrlwkrnhcnhRDYQN 336
Cdd:pfam00657   1 IVAFGDSLTDGGGDGP--------------------GGRFSWGDLLAD--FLARKLGVPGSGY------------NHGAN 46
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613988 337 ISRNGASSRN----LKKFIERKSD----PVPAMTT--------------PEKLYSNVMQTLKHLNSHLPN----GSHVIL 390
Cdd:pfam00657  47 FAIGGATIEDlpiqLEQLLRLISDvkdqAKPDLVTifigandlcnflssPARSKKRVPDLLDELRANLPQlglgARKFWV 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613988 391 YGLPdgtflwdnlhnryhPLGQLnkdmtyaqlysflnclqvsPCHGWMssnKTLRTLTSERAEQLSNTLKKIAAseKFTN 470
Cdd:pfam00657 127 HGLG--------------PLGCT-------------------PPKGCY---ELYNALAEEYNERLNELVNSLAA--AAED 168
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 2462613988 471 FNLFYMDFA-FHEIIQEWQKRGGQPwqliepvDGFHPNE 508
Cdd:pfam00657 169 ANVVYVDIYgFEDPTDPCCGIGLEP-------DGLHPSE 200
SapB_2 pfam03489
Saposin-like type B, region 2; Saposin B is a small non-enzymatic glycoprotein required for ...
81-114 9.90e-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: 42.56  E-value: 9.90e-06
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2462613988  81 TTCYLVIDKFGSDIIKLLSADMNADVVCHTLEFC 114
Cdd:pfam03489   1 DECKSLVDQYGPLIIDLLESELDPKDVCTALGLC 34
Cu-binding_MopE pfam11617
Putative metal-binding motif; The seqeunce of structure 2vov is not matched in any other ...
205-233 3.43e-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: 38.25  E-value: 3.43e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2462613988 205 DCNDSDESVYPGR--RPNNwdvhQDSNCNGI 233
Cdd:pfam11617   1 DCDDSDPAIHPGAaeICDG----IDNNCDGV 27
 
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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