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Conserved domains on  [gi|971393687|ref|XP_015131913|]
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N-acylethanolamine-hydrolyzing acid amidase isoform X2 [Gallus gallus]

Protein Classification

acid ceramidase family protein; Ntn hydrolase 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| Ntn (N-terminal nucleophile) hydrolase family protein is activated autocatalytically via an N-terminally located nucleophilic amino acid, and may catalyze the hydrolysis of amide bonds in either protein or small molecule substrates

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 ...
 115-343 8.11e-138

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: 390.87  E-value: 8.11e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971393687 115 NFAYESTAFCTSIIAQDDKGNIYHGRNLDYDFVDILSKITIDVQFIKSGQIAYRGTTFLGYVGLWTGQSPHKFTISGDER 194
Cdd:cd01903    1 NIFYEIFTFCTSIVAQDSNGTIYHARNLDFGFFEELSKLTVNVDFQRNGKIVFKGTTFAGYVGLLTGQKPGKFSLTINER 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971393687 195 EGGSWWENAIAAFLNR-NYPVSWLIRDTLSRAEDFQSAVLRLADIPIIAEVYYIVGGVSPKEGMVITRNRRGPADLWPLD 273
Cdd:cd01903   81 FSLDGGYNGILALLKKdGIPVSWLIRETLENATSYEDAVEKLSTTPILAPAYFIVGGVKPGEGVVITRNRDSVADVYPLD 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 971393687 274 PLGGAWFRVETNYDHWTTPPPCDDRRTPAMKALNATGQQNINFDTLFQVLSVKPVLNN-TVYTTVMSAAFP 343
Cdd:cd01903  161 LKNGTWFLVQTNYDRWKPPPFLDDRRTPAIKCMNALGQANISFKTLYDVLSTKPVLNKlTIYTTLMSVRTG 231
NAAA-beta pfam15508
beta subunit of N-acylethanolamine-hydrolyzing acid amidase; NAAA-beta is a family of ...
 33-89 6.51e-11

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: 57.25  E-value: 6.51e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 971393687   33 LCNVSLDSPAEERWLPVLRHFDPAF--LRAAVARVIDETVPKWFHDVIRPIAAELESFM 89
Cdd:pfam15508   5 WYVINLDLPPEERWTQVAKDYKPEIksLIPALKDLLKSLVPGKLVPLVDKLAADLLRYL 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 ...
 115-343 8.11e-138

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: 390.87  E-value: 8.11e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971393687 115 NFAYESTAFCTSIIAQDDKGNIYHGRNLDYDFVDILSKITIDVQFIKSGQIAYRGTTFLGYVGLWTGQSPHKFTISGDER 194
Cdd:cd01903    1 NIFYEIFTFCTSIVAQDSNGTIYHARNLDFGFFEELSKLTVNVDFQRNGKIVFKGTTFAGYVGLLTGQKPGKFSLTINER 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971393687 195 EGGSWWENAIAAFLNR-NYPVSWLIRDTLSRAEDFQSAVLRLADIPIIAEVYYIVGGVSPKEGMVITRNRRGPADLWPLD 273
Cdd:cd01903   81 FSLDGGYNGILALLKKdGIPVSWLIRETLENATSYEDAVEKLSTTPILAPAYFIVGGVKPGEGVVITRNRDSVADVYPLD 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 971393687 274 PLGGAWFRVETNYDHWTTPPPCDDRRTPAMKALNATGQQNINFDTLFQVLSVKPVLNN-TVYTTVMSAAFP 343
Cdd:cd01903  161 LKNGTWFLVQTNYDRWKPPPFLDDRRTPAIKCMNALGQANISFKTLYDVLSTKPVLNKlTIYTTLMSVRTG 231
C45_proenzyme NF040521
C45 family autoproteolytic acyltransferase/hydolase; Members of this family include hydrolases ...
 56-341 5.69e-13

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: 68.85  E-value: 5.69e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971393687  56 AFLRAAVARVIDETVPKWFH-------DVIRPIAAELESFMPQpFAGEIRGLCEALGVSLGDGVLLNFAYESTAF---CT 125
Cdd:NF040521  13 ELLKELIRDLYLALLRAWGLvswrelrDFAKEFLAALEAFAPE-LWEELEGIADGLGLPFEDVLALNARTEILAApdgCS 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971393687 126 SIIAQDDKGNIYHGRNLDYDfvDILSKITIDVQFIKSGQIAYRGTTFLGYV-GLWTGQSPHKFTISGDEREGGSWWENAI 204
Cdd:NF040521  92 TFAVLGEDGEPILARNYDWH--PELYDGCLLLTIRPDGGPRYASIGYAGLLpGRTDGMNEAGLAVTLNFLDGRKLPGVGV 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971393687 205 aaflnrnyPVSWLIRDTLSRAEDFQSAVLRLADIPIIAEVYYIVGG---------VSPKEgMVITRNRRGPAdlwpldpl 275
Cdd:NF040521 170 --------PVHLLARAILENCKTVDEAIALLKEIPRASSFNLTLADasgraasveASPDR-VVVVRPEDGLL-------- 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971393687 276 ggawfrVETNydHWTTPPPCDDRRTPA------MKALNATGQQNINFDTLFQVLS---VKPVLN---------NTVYTTV 337
Cdd:NF040521 233 ------VHTN--HFLSPELEEENRIATpssrerYERLEELLKGKLDAEDAKALLSdgyPLPICRhpypdgdrfGTLATVV 304


                 ....
gi 971393687 338 MSAA 341
Cdd:NF040521 305 FDPA 308
NAAA-beta pfam15508
beta subunit of N-acylethanolamine-hydrolyzing acid amidase; NAAA-beta is a family of ...
 33-89 6.51e-11

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: 57.25  E-value: 6.51e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 971393687   33 LCNVSLDSPAEERWLPVLRHFDPAF--LRAAVARVIDETVPKWFHDVIRPIAAELESFM 89
Cdd:pfam15508   5 WYVINLDLPPEERWTQVAKDYKPEIksLIPALKDLLKSLVPGKLVPLVDKLAADLLRYL 63
CBAH pfam02275
Linear amide C-N hydrolases, choloylglycine hydrolase family; This family includes several ...
 124-340 1.87e-09

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: 58.29  E-value: 1.87e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971393687  124 CTSIIAQDDKGNIYHGRNLDYDFvDILSKITIDVQFIK-SGQIAYRGTTFL-GYVGLWTGQSPHK-FTISGDEREGG--- 197
Cdd:pfam02275   1 CTSITLETKKGNLLFGRNMDFGI-SYGEEVIITPRNYKlVFEKLGNMLVTKyAVIGMGTDVGSYPlFYDGLNEKGLGiag 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971393687  198 -------SWWENAIAAflNRNYPVSWLIRDTLSRAEDFQSAVLRLADIPIIAEVYYIVGGVSP----------------- 253
Cdd:pfam02275  80 lyfpgyaFYSKGPKKD--KVNIQPGELILWVLGNFTSVEEVKELLTKLNIVNEALDILGGKAPlhwiisdasgesiviep 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971393687  254 -KEGMVITRNRRGpadlwpLDPLGGAWFRVETNYDHWTTPPPC-------DDRR-----------------TPAM----- 303
Cdd:pfam02275 158 rKEGLKVYDNEVG------VMTNSPTFDWHLTNLNNYTGLRPNqpqnffmGDLDltpfgqgtgglglpgdfTPASrfvra 231

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 971393687  304 ----KALNATGQQNINFDTLFQVLSVKP-----VLN------NTVYTTVMSA 340
Cdd:pfam02275 232 aylkMNLPKAKTETESVATFFHILSNVAipkgaVLNiegkleYTVYTSCMDL 283
 
Name Accession Description Interval E-value
Ntn_AC_NAAA cd01903
AC_NAAA This conserved domain includes two closely related proteins, acid ceramidase (AC, also ...
 115-343 8.11e-138

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: 390.87  E-value: 8.11e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971393687 115 NFAYESTAFCTSIIAQDDKGNIYHGRNLDYDFVDILSKITIDVQFIKSGQIAYRGTTFLGYVGLWTGQSPHKFTISGDER 194
Cdd:cd01903    1 NIFYEIFTFCTSIVAQDSNGTIYHARNLDFGFFEELSKLTVNVDFQRNGKIVFKGTTFAGYVGLLTGQKPGKFSLTINER 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971393687 195 EGGSWWENAIAAFLNR-NYPVSWLIRDTLSRAEDFQSAVLRLADIPIIAEVYYIVGGVSPKEGMVITRNRRGPADLWPLD 273
Cdd:cd01903   81 FSLDGGYNGILALLKKdGIPVSWLIRETLENATSYEDAVEKLSTTPILAPAYFIVGGVKPGEGVVITRNRDSVADVYPLD 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 971393687 274 PLGGAWFRVETNYDHWTTPPPCDDRRTPAMKALNATGQQNINFDTLFQVLSVKPVLNN-TVYTTVMSAAFP 343
Cdd:cd01903  161 LKNGTWFLVQTNYDRWKPPPFLDDRRTPAIKCMNALGQANISFKTLYDVLSTKPVLNKlTIYTTLMSVRTG 231
Ntn_CGH_like cd01935
Choloylglycine hydrolase (CGH)_like. This family of choloylglycine hydrolase-like proteins ...
 124-339 4.07e-50

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: 167.15  E-value: 4.07e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971393687 124 CTSIIAQDDKGNIYHGRNLDYDFVDILSKITIDVQFIKSGQI---------AYRGTTFLGYVGLWTGQSPHKFTISGDER 194
Cdd:cd01935    1 CTSIVAQTKDGGVYLGRNMDFSFDYELRLLVFPRGYQRNGQTgdkskwyakYGSGGTSAGYIGLVDGMNEKGLSVSLLYF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971393687 195 EGGSWWENAIAAFlNRNYPVSWLIRDTLSRAEDFQSAVLRLADIPII----------AEVYYIVGGVSpKEGMVITRNRR 264
Cdd:cd01935   81 PGYAYYPAGIKEG-KDGLPAFELIRWVLENCDSVEEVKEALKKIPIVdfpiplggpaAPLHYILSDKS-GDSAVIEPIDG 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971393687 265 GPADLWPLdplggaWFRVETNYDHWTTPPPcddRRTPAMKALNATGQQN----INFDTLFQVLSVKPVLNN-TVYTTVMS 339
Cdd:cd01935  159 GLKIYDNP------WFGVMTNHPTFDWHLP---RRFVRVAYLKNTAQKNketvEDVKNLFHILESVPIPNGlTVYTTVMD 229
C45_proenzyme NF040521
C45 family autoproteolytic acyltransferase/hydolase; Members of this family include hydrolases ...
 56-341 5.69e-13

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: 68.85  E-value: 5.69e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971393687  56 AFLRAAVARVIDETVPKWFH-------DVIRPIAAELESFMPQpFAGEIRGLCEALGVSLGDGVLLNFAYESTAF---CT 125
Cdd:NF040521  13 ELLKELIRDLYLALLRAWGLvswrelrDFAKEFLAALEAFAPE-LWEELEGIADGLGLPFEDVLALNARTEILAApdgCS 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971393687 126 SIIAQDDKGNIYHGRNLDYDfvDILSKITIDVQFIKSGQIAYRGTTFLGYV-GLWTGQSPHKFTISGDEREGGSWWENAI 204
Cdd:NF040521  92 TFAVLGEDGEPILARNYDWH--PELYDGCLLLTIRPDGGPRYASIGYAGLLpGRTDGMNEAGLAVTLNFLDGRKLPGVGV 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971393687 205 aaflnrnyPVSWLIRDTLSRAEDFQSAVLRLADIPIIAEVYYIVGG---------VSPKEgMVITRNRRGPAdlwpldpl 275
Cdd:NF040521 170 --------PVHLLARAILENCKTVDEAIALLKEIPRASSFNLTLADasgraasveASPDR-VVVVRPEDGLL-------- 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971393687 276 ggawfrVETNydHWTTPPPCDDRRTPA------MKALNATGQQNINFDTLFQVLS---VKPVLN---------NTVYTTV 337
Cdd:NF040521 233 ------VHTN--HFLSPELEEENRIATpssrerYERLEELLKGKLDAEDAKALLSdgyPLPICRhpypdgdrfGTLATVV 304


                 ....
gi 971393687 338 MSAA 341
Cdd:NF040521 305 FDPA 308
NAAA-beta pfam15508
beta subunit of N-acylethanolamine-hydrolyzing acid amidase; NAAA-beta is a family of ...
 33-89 6.51e-11

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: 57.25  E-value: 6.51e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 971393687   33 LCNVSLDSPAEERWLPVLRHFDPAF--LRAAVARVIDETVPKWFHDVIRPIAAELESFM 89
Cdd:pfam15508   5 WYVINLDLPPEERWTQVAKDYKPEIksLIPALKDLLKSLVPGKLVPLVDKLAADLLRYL 63
CBAH pfam02275
Linear amide C-N hydrolases, choloylglycine hydrolase family; This family includes several ...
 124-340 1.87e-09

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: 58.29  E-value: 1.87e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971393687  124 CTSIIAQDDKGNIYHGRNLDYDFvDILSKITIDVQFIK-SGQIAYRGTTFL-GYVGLWTGQSPHK-FTISGDEREGG--- 197
Cdd:pfam02275   1 CTSITLETKKGNLLFGRNMDFGI-SYGEEVIITPRNYKlVFEKLGNMLVTKyAVIGMGTDVGSYPlFYDGLNEKGLGiag 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971393687  198 -------SWWENAIAAflNRNYPVSWLIRDTLSRAEDFQSAVLRLADIPIIAEVYYIVGGVSP----------------- 253
Cdd:pfam02275  80 lyfpgyaFYSKGPKKD--KVNIQPGELILWVLGNFTSVEEVKELLTKLNIVNEALDILGGKAPlhwiisdasgesiviep 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 971393687  254 -KEGMVITRNRRGpadlwpLDPLGGAWFRVETNYDHWTTPPPC-------DDRR-----------------TPAM----- 303
Cdd:pfam02275 158 rKEGLKVYDNEVG------VMTNSPTFDWHLTNLNNYTGLRPNqpqnffmGDLDltpfgqgtgglglpgdfTPASrfvra 231

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 971393687  304 ----KALNATGQQNINFDTLFQVLSVKP-----VLN------NTVYTTVMSA 340
Cdd:pfam02275 232 aylkMNLPKAKTETESVATFFHILSNVAipkgaVLNiegkleYTVYTSCMDL 283
Ntn_PVA cd00542
Penicillin V acylase (PVA), also known as conjugated bile salt acid hydrolase (CBAH), ...
 124-155 5.43e-03

Penicillin V acylase (PVA), also known as conjugated bile salt acid hydrolase (CBAH), catalyzes the hydrolysis of penicillin V to yield 6-amino penicillanic acid (6-APA), an important key intermediate of semisynthetic penicillins. PVA has an N-terminal nucleophilic cysteine, as do other members of the Ntn hydrolase family to which PVA belongs. This nucleophilic cysteine is exposed by post-translational prossessing of the PVA precursor. PVA forms a homotetramer.


Pssm-ID: 238303  Cd Length: 303  Bit Score: 38.35  E-value: 5.43e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 971393687 124 CTSIIAQDDKGNIYHGRNLDYDFvDILSKITI 155
Cdd:cd00542    1 CTSLTLSTKDGDHVFGRTMDFAF-DLGSQIII 31
 
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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