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Conserved domains on  [gi|118442845|ref|NP_001072984|]
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putative inactive neutral ceramidase B isoform 1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ceramidse_alk_C pfam17048
Neutral/alkaline non-lysosomal ceramidase, C-terminal; This family represents C-terminal ...
 30-162 2.78e-58

Neutral/alkaline non-lysosomal ceramidase, C-terminal; This family represents C-terminal domain of a group of neutral/alkaline ceramidases found in both bacteria and eukaryotes. The EC classification is EC:3.5.1.23. The enzyme hydrolyses ceramide to generate sphingosine and fatty acid. The enzyme plays a regulatory role in a variety of physiological events in eukaryotes and also functions as an exotoxin in particular bacteria. This C-terminal tail of the enzyme is highly conserved across all species and may play a role in the interaction of the enzyme with the plasma membranes. The tail is also vital for the stabilization of the enzyme as a whole.


:

Pssm-ID: 465340 [Multi-domain]  Cd Length: 165  Bit Score: 178.89  E-value: 2.78e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442845   30 IVDRAPKGRTFGDVLQPAKPEYRVGEVAEVIFVGANPKNSvqNQTHQTFLTVEKYEATSTsWQIVCNDASWETRFYWHK- 108
Cdd:pfam17048  37 VFDTPPLGKSFGDVLTDPNPSYRRGDTVSVTFVGANPRNN--LRLEGTFLAVERLVDGGT-WTTVRDDADWSTRFHWKRt 113

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 118442845  109 -GLLGLSNATVEWHIPDTAQPGIYRIRYFGHNRKQDILKpavILSFEGTSPAFEV 162
Cdd:pfam17048 114 sGLLGTSEVTIEWEIPADTPPGTYRIRYFGDSKSLLGGS---ITPFEGTSSSFTV 165
 
Name Accession Description Interval E-value
Ceramidse_alk_C pfam17048
Neutral/alkaline non-lysosomal ceramidase, C-terminal; This family represents C-terminal ...
 30-162 2.78e-58

Neutral/alkaline non-lysosomal ceramidase, C-terminal; This family represents C-terminal domain of a group of neutral/alkaline ceramidases found in both bacteria and eukaryotes. The EC classification is EC:3.5.1.23. The enzyme hydrolyses ceramide to generate sphingosine and fatty acid. The enzyme plays a regulatory role in a variety of physiological events in eukaryotes and also functions as an exotoxin in particular bacteria. This C-terminal tail of the enzyme is highly conserved across all species and may play a role in the interaction of the enzyme with the plasma membranes. The tail is also vital for the stabilization of the enzyme as a whole.


Pssm-ID: 465340 [Multi-domain]  Cd Length: 165  Bit Score: 178.89  E-value: 2.78e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442845   30 IVDRAPKGRTFGDVLQPAKPEYRVGEVAEVIFVGANPKNSvqNQTHQTFLTVEKYEATSTsWQIVCNDASWETRFYWHK- 108
Cdd:pfam17048  37 VFDTPPLGKSFGDVLTDPNPSYRRGDTVSVTFVGANPRNN--LRLEGTFLAVERLVDGGT-WTTVRDDADWSTRFHWKRt 113

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 118442845  109 -GLLGLSNATVEWHIPDTAQPGIYRIRYFGHNRKQDILKpavILSFEGTSPAFEV 162
Cdd:pfam17048 114 sGLLGTSEVTIEWEIPADTPPGTYRIRYFGDSKSLLGGS---ITPFEGTSSSFTV 165
PTZ00487 PTZ00487
ceramidase; Provisional
 30-163 3.71e-29

ceramidase; Provisional


Pssm-ID: 240437 [Multi-domain]  Cd Length: 715  Bit Score: 111.94  E-value: 3.71e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442845  30 IVDRAPKGRTFGDVLQPAKPE--YRVGEVAEVIFVGANPKNSVQnqTHQTFLTVEKYEATStSWQIVCNDASWETRFYWH 107
Cdd:PTZ00487 585 IVDSAPFFDDFGDLYQDVDTEkvYSNNDTVSAEFYGGNPRNNFM--TESSFLTVDKLNEKN-QWTTILVDGDWDTKWHWK 661

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 118442845 108 KGLLGLSNATVEWHIPDTAQPGIYRIRYFGHNRKQDIlkPAVILSFEGTSPAFEVV 163
Cdd:PTZ00487 662 MHDLGFSLITIIWSIGPTTEPGTYRITHSGYAKKNPF--SQNLTPYQGISSNFKVQ 715
 
Name Accession Description Interval E-value
Ceramidse_alk_C pfam17048
Neutral/alkaline non-lysosomal ceramidase, C-terminal; This family represents C-terminal ...
 30-162 2.78e-58

Neutral/alkaline non-lysosomal ceramidase, C-terminal; This family represents C-terminal domain of a group of neutral/alkaline ceramidases found in both bacteria and eukaryotes. The EC classification is EC:3.5.1.23. The enzyme hydrolyses ceramide to generate sphingosine and fatty acid. The enzyme plays a regulatory role in a variety of physiological events in eukaryotes and also functions as an exotoxin in particular bacteria. This C-terminal tail of the enzyme is highly conserved across all species and may play a role in the interaction of the enzyme with the plasma membranes. The tail is also vital for the stabilization of the enzyme as a whole.


Pssm-ID: 465340 [Multi-domain]  Cd Length: 165  Bit Score: 178.89  E-value: 2.78e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442845   30 IVDRAPKGRTFGDVLQPAKPEYRVGEVAEVIFVGANPKNSvqNQTHQTFLTVEKYEATSTsWQIVCNDASWETRFYWHK- 108
Cdd:pfam17048  37 VFDTPPLGKSFGDVLTDPNPSYRRGDTVSVTFVGANPRNN--LRLEGTFLAVERLVDGGT-WTTVRDDADWSTRFHWKRt 113

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 118442845  109 -GLLGLSNATVEWHIPDTAQPGIYRIRYFGHNRKQDILKpavILSFEGTSPAFEV 162
Cdd:pfam17048 114 sGLLGTSEVTIEWEIPADTPPGTYRIRYFGDSKSLLGGS---ITPFEGTSSSFTV 165
PTZ00487 PTZ00487
ceramidase; Provisional
 30-163 3.71e-29

ceramidase; Provisional


Pssm-ID: 240437 [Multi-domain]  Cd Length: 715  Bit Score: 111.94  E-value: 3.71e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442845  30 IVDRAPKGRTFGDVLQPAKPE--YRVGEVAEVIFVGANPKNSVQnqTHQTFLTVEKYEATStSWQIVCNDASWETRFYWH 107
Cdd:PTZ00487 585 IVDSAPFFDDFGDLYQDVDTEkvYSNNDTVSAEFYGGNPRNNFM--TESSFLTVDKLNEKN-QWTTILVDGDWDTKWHWK 661

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 118442845 108 KGLLGLSNATVEWHIPDTAQPGIYRIRYFGHNRKQDIlkPAVILSFEGTSPAFEVV 163
Cdd:PTZ00487 662 MHDLGFSLITIIWSIGPTTEPGTYRITHSGYAKKNPF--SQNLTPYQGISSNFKVQ 715
 
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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