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Conserved domains on  [gi|530377541|ref|XP_005262980|]
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N-acylethanolamine-hydrolyzing acid amidase isoform X7 [Homo sapiens]

Protein Classification

acid ceramidase family protein( domain architecture ID 10634631)

acid ceramidase (AC) family protein similar to AC, which catalyzes the hydrolysis of ceramide to sphingosine and fatty acid, and to N-acylethanolamine-hydrolyzing acid amidase (NAAA), that that hydrolyzes bioactive N-acylethanolamines to fatty acids and ethanolamine at acidic pH

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ntn_AC_NAAA cd01903
AC_NAAA This conserved domain includes two closely related proteins, acid ceramidase (AC, also ...
 117-333 1.44e-131

AC_NAAA This conserved domain includes two closely related proteins, acid ceramidase (AC, also known as N-acylsphingosine amidohydrolase), and N-acylethanolamine-hydrolyzing acid amidase (NAAA). AC catalyzes the hydrolysis of ceramide to sphingosine and fatty acid. Ceramide is required for the biosynthesis of most sphingolipids and plays an important role in many signal transduction pathways by inducing apoptosis and/or arresting cell growth. An inherited deficiency of AC activity leads to the lysosomal storage disorder known as Farber disease. AC is considered a "rheostat" important for maintaining the proper intracellular levels of these lipids since hydrolysis of ceramide is the only source of sphingosine in cells. NAAA is a eukaryotic glycoprotein that hydrolyzes bioactive N-acylethanolamines, including anandamide (an endocannabinoid) and N-palmitoylethanolamine (an anti-inflammatory and neuroprotective substance), to fatty acids and ethanolamine at acidic pH. NAAA shows structural and functional similarity to acid ceramidase, but lacks the ceramide-hydrolyzing activity of AC.


:

Pssm-ID: 238886  Cd Length: 231  Bit Score: 374.30  E-value: 1.44e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377541 117 NLAYESSVFCTSIVAQDSRGHIYHGRNLDYPFGNVLRKLTVDVQFLKNGQIAFTGTTFIGYVGLWTGQSPHKFTVSGDER 196
Cdd:cd01903    1 NIFYEIFTFCTSIVAQDSNGTIYHARNLDFGFFEELSKLTVNVDFQRNGKIVFKGTTFAGYVGLLTGQKPGKFSLTINER 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377541 197 DKGWWWENAI-AALFRRHIPVSWLIRATLSESENFEAAVGKLAKTPLIADVYYIVGGTSPREGVVITRNRDGPADIWPLD 275
Cdd:cd01903   81 FSLDGGYNGIlALLKKDGIPVSWLIRETLENATSYEDAVEKLSTTPILAPAYFIVGGVKPGEGVVITRNRDSVADVYPLD 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 530377541 276 PLNGAWFRVETNYDHWKPAPKEDDRRTSAIKALNATGQANLSLEALFQILSVVPVYNK 333
Cdd:cd01903  161 LKNGTWFLVQTNYDRWKPPPFLDDRRTPAIKCMNALGQANISFKTLYDVLSTKPVLNK 218
NAAA-beta pfam15508
beta subunit of N-acylethanolamine-hydrolyzing acid amidase; NAAA-beta is a family of ...
 32-91 3.70e-12

beta subunit of N-acylethanolamine-hydrolyzing acid amidase; NAAA-beta is a family of vertebral sequences that form the beta subunit of vertebral N-acylethanolamine-hydrolyzing acid amidase, a member of the choloylglycine hydrolase acid ceramidase family. The alpha subunit is represented by family CBAH, pfam02275.


:

Pssm-ID: 464754  Cd Length: 63  Bit Score: 60.72  E-value: 3.70e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530377541   32 AAPRFNVSLDSVPELRWLPVLRHYD--LDLVRAAMAQVIGDRVPKWVHVLIGKVVLELERFL 91
Cdd:pfam15508   2 PVPWYVINLDLPPEERWTQVAKDYKpeIKSLIPALKDLLKSLVPGKLVPLVDKLAADLLRYL 63
 
Name Accession Description Interval E-value
Ntn_AC_NAAA cd01903
AC_NAAA This conserved domain includes two closely related proteins, acid ceramidase (AC, also ...
 117-333 1.44e-131

AC_NAAA This conserved domain includes two closely related proteins, acid ceramidase (AC, also known as N-acylsphingosine amidohydrolase), and N-acylethanolamine-hydrolyzing acid amidase (NAAA). AC catalyzes the hydrolysis of ceramide to sphingosine and fatty acid. Ceramide is required for the biosynthesis of most sphingolipids and plays an important role in many signal transduction pathways by inducing apoptosis and/or arresting cell growth. An inherited deficiency of AC activity leads to the lysosomal storage disorder known as Farber disease. AC is considered a "rheostat" important for maintaining the proper intracellular levels of these lipids since hydrolysis of ceramide is the only source of sphingosine in cells. NAAA is a eukaryotic glycoprotein that hydrolyzes bioactive N-acylethanolamines, including anandamide (an endocannabinoid) and N-palmitoylethanolamine (an anti-inflammatory and neuroprotective substance), to fatty acids and ethanolamine at acidic pH. NAAA shows structural and functional similarity to acid ceramidase, but lacks the ceramide-hydrolyzing activity of AC.


Pssm-ID: 238886  Cd Length: 231  Bit Score: 374.30  E-value: 1.44e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377541 117 NLAYESSVFCTSIVAQDSRGHIYHGRNLDYPFGNVLRKLTVDVQFLKNGQIAFTGTTFIGYVGLWTGQSPHKFTVSGDER 196
Cdd:cd01903    1 NIFYEIFTFCTSIVAQDSNGTIYHARNLDFGFFEELSKLTVNVDFQRNGKIVFKGTTFAGYVGLLTGQKPGKFSLTINER 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377541 197 DKGWWWENAI-AALFRRHIPVSWLIRATLSESENFEAAVGKLAKTPLIADVYYIVGGTSPREGVVITRNRDGPADIWPLD 275
Cdd:cd01903   81 FSLDGGYNGIlALLKKDGIPVSWLIRETLENATSYEDAVEKLSTTPILAPAYFIVGGVKPGEGVVITRNRDSVADVYPLD 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 530377541 276 PLNGAWFRVETNYDHWKPAPKEDDRRTSAIKALNATGQANLSLEALFQILSVVPVYNK 333
Cdd:cd01903  161 LKNGTWFLVQTNYDRWKPPPFLDDRRTPAIKCMNALGQANISFKTLYDVLSTKPVLNK 218
C45_proenzyme NF040521
C45 family autoproteolytic acyltransferase/hydolase; Members of this family include hydrolases ...
 59-326 2.63e-12

C45 family autoproteolytic acyltransferase/hydolase; Members of this family include hydrolases and N-acyltransferases, and belong to the Ntn (N-terminal nucleophile) hydrolase family. Members have an invariant Cys residue (Cys-103 in XP_002569112.1) required both for autoproteolytic processing into alpha and beta chains and for activity. The family is described by MEROPs as a cysteine protease, family C45, because of its autoproteolytic activity. Characterized members include TAN from Drosophila, which removes beta-alanine from both carcinine and N-beta-alanyl dopamine, and isopenicillin-N N-acyltransferase from various fungi. The latter has been heavily studied because of its role in penicillin biosynthesis.


Pssm-ID: 468523 [Multi-domain]  Cd Length: 312  Bit Score: 66.54  E-value: 2.63e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377541  59 LVRAAMAQVIGDRVPKWVHV-------LIGKVVLELERFLPQpFTGEIRGMCDFMNLSLADCLLVNLAYE---SSVFCTS 128
Cdd:NF040521  14 LLKELIRDLYLALLRAWGLVswrelrdFAKEFLAALEAFAPE-LWEELEGIADGLGLPFEDVLALNARTEilaAPDGCST 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377541 129 IVAQDSRGHIYHGRNLDYPFGnvLRKLTVDVQFLKNGQIAFtgtTFIGYVGLWTGQS----PHKFTVSGDERDKGWWWEN 204
Cdd:NF040521  93 FAVLGEDGEPILARNYDWHPE--LYDGCLLLTIRPDGGPRY---ASIGYAGLLPGRTdgmnEAGLAVTLNFLDGRKLPGV 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377541 205 AiaalfrrhIPVSWLIRATLSESENFEAAVGKLAKTPLIADVYYIVgGTSPREGVVITRNrdgPADIWPLDPLNGawFRV 284
Cdd:NF040521 168 G--------VPVHLLARAILENCKTVDEAIALLKEIPRASSFNLTL-ADASGRAASVEAS---PDRVVVVRPEDG--LLV 233

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 530377541 285 ETNydHW---KPAPKEDDRRTSAIK---ALNATGQANLSLEALFQILS 326
Cdd:NF040521 234 HTN--HFlspELEEENRIATPSSREryeRLEELLKGKLDAEDAKALLS 279
NAAA-beta pfam15508
beta subunit of N-acylethanolamine-hydrolyzing acid amidase; NAAA-beta is a family of ...
 32-91 3.70e-12

beta subunit of N-acylethanolamine-hydrolyzing acid amidase; NAAA-beta is a family of vertebral sequences that form the beta subunit of vertebral N-acylethanolamine-hydrolyzing acid amidase, a member of the choloylglycine hydrolase acid ceramidase family. The alpha subunit is represented by family CBAH, pfam02275.


Pssm-ID: 464754  Cd Length: 63  Bit Score: 60.72  E-value: 3.70e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530377541   32 AAPRFNVSLDSVPELRWLPVLRHYD--LDLVRAAMAQVIGDRVPKWVHVLIGKVVLELERFL 91
Cdd:pfam15508   2 PVPWYVINLDLPPEERWTQVAKDYKpeIKSLIPALKDLLKSLVPGKLVPLVDKLAADLLRYL 63
CBAH pfam02275
Linear amide C-N hydrolases, choloylglycine hydrolase family; This family includes several ...
 126-330 9.84e-11

Linear amide C-N hydrolases, choloylglycine hydrolase family; This family includes several hydrolases which cleave carbon-nitrogen bonds, other than peptide bonds, in linear amides. These include choloylglycine hydrolase (conjugated bile acid hydrolase, CBAH) EC:3.5.1.24, penicillin acylase EC:3.5.1.11 and acid ceramidase EC:3.5.1.23. This domain forms the alpha-subunit for members from vertebral species, see family NAAA-beta, pfam15508.


Pssm-ID: 396726  Cd Length: 316  Bit Score: 61.76  E-value: 9.84e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377541  126 CTSIVAQDSRGHIYHGRNLDYPFGN----VLRKLTVDVQFLKNGQIAFTGTTFIGyVGLWTGQSPhKFTVSGDERDKGww 201
Cdd:pfam02275   1 CTSITLETKKGNLLFGRNMDFGISYgeevIITPRNYKLVFEKLGNMLVTKYAVIG-MGTDVGSYP-LFYDGLNEKGLG-- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377541  202 wenaIAALF--------------RRHIPVSWLIRATLSESENFEAAVGKLAKTPLIADVYYIVGGTSPR---------EG 258
Cdd:pfam02275  77 ----IAGLYfpgyafyskgpkkdKVNIQPGELILWVLGNFTSVEEVKELLTKLNIVNEALDILGGKAPLhwiisdasgES 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377541  259 VVItRNRDGPADIWPLDPL----NGAWFRVETNYDHWK-------PAPKEDDRRTSAI---------------------- 305
Cdd:pfam02275 153 IVI-EPRKEGLKVYDNEVGvmtnSPTFDWHLTNLNNYTglrpnqpQNFFMGDLDLTPFgqgtgglglpgdftpasrfvra 231

                         250       260
                  ....*....|....*....|....*....
gi 530377541  306 ----KALNATGQANLSLEALFQILSVVPV 330
Cdd:pfam02275 232 aylkMNLPKAKTETESVATFFHILSNVAI 260
 
Name Accession Description Interval E-value
Ntn_AC_NAAA cd01903
AC_NAAA This conserved domain includes two closely related proteins, acid ceramidase (AC, also ...
 117-333 1.44e-131

AC_NAAA This conserved domain includes two closely related proteins, acid ceramidase (AC, also known as N-acylsphingosine amidohydrolase), and N-acylethanolamine-hydrolyzing acid amidase (NAAA). AC catalyzes the hydrolysis of ceramide to sphingosine and fatty acid. Ceramide is required for the biosynthesis of most sphingolipids and plays an important role in many signal transduction pathways by inducing apoptosis and/or arresting cell growth. An inherited deficiency of AC activity leads to the lysosomal storage disorder known as Farber disease. AC is considered a "rheostat" important for maintaining the proper intracellular levels of these lipids since hydrolysis of ceramide is the only source of sphingosine in cells. NAAA is a eukaryotic glycoprotein that hydrolyzes bioactive N-acylethanolamines, including anandamide (an endocannabinoid) and N-palmitoylethanolamine (an anti-inflammatory and neuroprotective substance), to fatty acids and ethanolamine at acidic pH. NAAA shows structural and functional similarity to acid ceramidase, but lacks the ceramide-hydrolyzing activity of AC.


Pssm-ID: 238886  Cd Length: 231  Bit Score: 374.30  E-value: 1.44e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377541 117 NLAYESSVFCTSIVAQDSRGHIYHGRNLDYPFGNVLRKLTVDVQFLKNGQIAFTGTTFIGYVGLWTGQSPHKFTVSGDER 196
Cdd:cd01903    1 NIFYEIFTFCTSIVAQDSNGTIYHARNLDFGFFEELSKLTVNVDFQRNGKIVFKGTTFAGYVGLLTGQKPGKFSLTINER 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377541 197 DKGWWWENAI-AALFRRHIPVSWLIRATLSESENFEAAVGKLAKTPLIADVYYIVGGTSPREGVVITRNRDGPADIWPLD 275
Cdd:cd01903   81 FSLDGGYNGIlALLKKDGIPVSWLIRETLENATSYEDAVEKLSTTPILAPAYFIVGGVKPGEGVVITRNRDSVADVYPLD 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 530377541 276 PLNGAWFRVETNYDHWKPAPKEDDRRTSAIKALNATGQANLSLEALFQILSVVPVYNK 333
Cdd:cd01903  161 LKNGTWFLVQTNYDRWKPPPFLDDRRTPAIKCMNALGQANISFKTLYDVLSTKPVLNK 218
Ntn_CGH_like cd01935
Choloylglycine hydrolase (CGH)_like. This family of choloylglycine hydrolase-like proteins ...
 126-333 1.38e-44

Choloylglycine hydrolase (CGH)_like. This family of choloylglycine hydrolase-like proteins includes conjugated bile acid hydrolase (CBAH), penicillin V acylase (PVA), acid ceramidase (AC), and N-acylethanolamine-hydrolyzing acid amidase (NAAA) which cleave non-peptide carbon-nitrogen bonds in bile salt constituents. These enzymes have an N-terminal nucleophilic cysteine, as do other members of the Ntn hydrolase family to which they belong. This nucleophilic cysteine is exposed by post-translational prossessing of the precursor protein.


Pssm-ID: 238910  Cd Length: 229  Bit Score: 152.12  E-value: 1.38e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377541 126 CTSIVAQDSRGHIYHGRNLDYPFGNVLRKLTVDVQFLKNGQI---------AFTGTTFIGYVGLWTGQSPHKFTVSGDER 196
Cdd:cd01935    1 CTSIVAQTKDGGVYLGRNMDFSFDYELRLLVFPRGYQRNGQTgdkskwyakYGSGGTSAGYIGLVDGMNEKGLSVSLLYF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377541 197 DKGWWWENAIAAlFRRHIPVSWLIRATLSESENFEAAVGKLAKTPLI----------ADVYYIVGGTSpREGVVITRNRD 266
Cdd:cd01935   81 PGYAYYPAGIKE-GKDGLPAFELIRWVLENCDSVEEVKEALKKIPIVdfpiplggpaAPLHYILSDKS-GDSAVIEPIDG 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530377541 267 GPADIWPLdplngaWFRVETNYDHWKPAPkedDRRTSAIKALNATGQANL----SLEALFQILSVVPVYNK 333
Cdd:cd01935  159 GLKIYDNP------WFGVMTNHPTFDWHL---PRRFVRVAYLKNTAQKNKetveDVKNLFHILESVPIPNG 220
C45_proenzyme NF040521
C45 family autoproteolytic acyltransferase/hydolase; Members of this family include hydrolases ...
 59-326 2.63e-12

C45 family autoproteolytic acyltransferase/hydolase; Members of this family include hydrolases and N-acyltransferases, and belong to the Ntn (N-terminal nucleophile) hydrolase family. Members have an invariant Cys residue (Cys-103 in XP_002569112.1) required both for autoproteolytic processing into alpha and beta chains and for activity. The family is described by MEROPs as a cysteine protease, family C45, because of its autoproteolytic activity. Characterized members include TAN from Drosophila, which removes beta-alanine from both carcinine and N-beta-alanyl dopamine, and isopenicillin-N N-acyltransferase from various fungi. The latter has been heavily studied because of its role in penicillin biosynthesis.


Pssm-ID: 468523 [Multi-domain]  Cd Length: 312  Bit Score: 66.54  E-value: 2.63e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377541  59 LVRAAMAQVIGDRVPKWVHV-------LIGKVVLELERFLPQpFTGEIRGMCDFMNLSLADCLLVNLAYE---SSVFCTS 128
Cdd:NF040521  14 LLKELIRDLYLALLRAWGLVswrelrdFAKEFLAALEAFAPE-LWEELEGIADGLGLPFEDVLALNARTEilaAPDGCST 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377541 129 IVAQDSRGHIYHGRNLDYPFGnvLRKLTVDVQFLKNGQIAFtgtTFIGYVGLWTGQS----PHKFTVSGDERDKGWWWEN 204
Cdd:NF040521  93 FAVLGEDGEPILARNYDWHPE--LYDGCLLLTIRPDGGPRY---ASIGYAGLLPGRTdgmnEAGLAVTLNFLDGRKLPGV 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377541 205 AiaalfrrhIPVSWLIRATLSESENFEAAVGKLAKTPLIADVYYIVgGTSPREGVVITRNrdgPADIWPLDPLNGawFRV 284
Cdd:NF040521 168 G--------VPVHLLARAILENCKTVDEAIALLKEIPRASSFNLTL-ADASGRAASVEAS---PDRVVVVRPEDG--LLV 233

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 530377541 285 ETNydHW---KPAPKEDDRRTSAIK---ALNATGQANLSLEALFQILS 326
Cdd:NF040521 234 HTN--HFlspELEEENRIATPSSREryeRLEELLKGKLDAEDAKALLS 279
NAAA-beta pfam15508
beta subunit of N-acylethanolamine-hydrolyzing acid amidase; NAAA-beta is a family of ...
 32-91 3.70e-12

beta subunit of N-acylethanolamine-hydrolyzing acid amidase; NAAA-beta is a family of vertebral sequences that form the beta subunit of vertebral N-acylethanolamine-hydrolyzing acid amidase, a member of the choloylglycine hydrolase acid ceramidase family. The alpha subunit is represented by family CBAH, pfam02275.


Pssm-ID: 464754  Cd Length: 63  Bit Score: 60.72  E-value: 3.70e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530377541   32 AAPRFNVSLDSVPELRWLPVLRHYD--LDLVRAAMAQVIGDRVPKWVHVLIGKVVLELERFL 91
Cdd:pfam15508   2 PVPWYVINLDLPPEERWTQVAKDYKpeIKSLIPALKDLLKSLVPGKLVPLVDKLAADLLRYL 63
CBAH pfam02275
Linear amide C-N hydrolases, choloylglycine hydrolase family; This family includes several ...
 126-330 9.84e-11

Linear amide C-N hydrolases, choloylglycine hydrolase family; This family includes several hydrolases which cleave carbon-nitrogen bonds, other than peptide bonds, in linear amides. These include choloylglycine hydrolase (conjugated bile acid hydrolase, CBAH) EC:3.5.1.24, penicillin acylase EC:3.5.1.11 and acid ceramidase EC:3.5.1.23. This domain forms the alpha-subunit for members from vertebral species, see family NAAA-beta, pfam15508.


Pssm-ID: 396726  Cd Length: 316  Bit Score: 61.76  E-value: 9.84e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377541  126 CTSIVAQDSRGHIYHGRNLDYPFGN----VLRKLTVDVQFLKNGQIAFTGTTFIGyVGLWTGQSPhKFTVSGDERDKGww 201
Cdd:pfam02275   1 CTSITLETKKGNLLFGRNMDFGISYgeevIITPRNYKLVFEKLGNMLVTKYAVIG-MGTDVGSYP-LFYDGLNEKGLG-- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377541  202 wenaIAALF--------------RRHIPVSWLIRATLSESENFEAAVGKLAKTPLIADVYYIVGGTSPR---------EG 258
Cdd:pfam02275  77 ----IAGLYfpgyafyskgpkkdKVNIQPGELILWVLGNFTSVEEVKELLTKLNIVNEALDILGGKAPLhwiisdasgES 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377541  259 VVItRNRDGPADIWPLDPL----NGAWFRVETNYDHWK-------PAPKEDDRRTSAI---------------------- 305
Cdd:pfam02275 153 IVI-EPRKEGLKVYDNEVGvmtnSPTFDWHLTNLNNYTglrpnqpQNFFMGDLDLTPFgqgtgglglpgdftpasrfvra 231

                         250       260
                  ....*....|....*....|....*....
gi 530377541  306 ----KALNATGQANLSLEALFQILSVVPV 330
Cdd:pfam02275 232 aylkMNLPKAKTETESVATFFHILSNVAI 260
 
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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