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Conserved domains on  [gi|119625123|gb|EAX04718|]
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signal peptidase complex subunit 3 homolog (S. cerevisiae), isoform CRA_a [Homo sapiens]

Protein Classification

signal peptidase complex subunit 3 family protein( domain architecture ID 10518971)

signal peptidase complex subunit 3 (SPCS3) family protein similar to SPCS3, a component of the microsomal signal peptidase complex which removes signal peptides and other N-terminal peptides from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SPC22 pfam04573
Signal peptidase subunit; Translocation of polypeptide chains across the endoplasmic reticulum ...
 1-173 4.16e-79

Signal peptidase subunit; Translocation of polypeptide chains across the endoplasmic reticulum membrane is triggered by signal sequences. During translocation of the nascent chain through the membrane, the signal sequence of most secretory and membrane proteins is cleaved off. Cleavage occurs by the signal peptidase complex (SPC) which consists of four subunits in yeast and five in mammals. This family is common to yeast and mammals.


:

Pssm-ID: 461357  Cd Length: 172  Bit Score: 232.84  E-value: 4.16e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625123    1 MNTVLSRANSLFAFSLSVMAALTFGCFITTAFKDRSvPVRLHVSRIMLKNVEDFTGPR-ERSDLGFITFDITADIQNIFD 79
Cdd:pfam04573   1 MHSLLQRLNAVSAFALTVLAVLCALIALSSLFQDTS-SISNIVPSVKVKNSRYYGSVRgKPKDNAKITFDLDADLSPLFN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625123   80 WNVKQLFLYLSAEYSTKNNALNQVVLWDKIVLRGDNPKLLLKDMKTKYFFFDDGNGLKGnRNVTLTLSWNVVPNAGILPL 159
Cdd:pfam04573  80 WNTKQLFVYLTAEYETKKNSVNQVVIWDKIIRSKEDAKLNLKNAKSKYSFWDDGNSLRG-RNVTLTLHWNVMPWVGLLPY 158

                         170
                  ....*....|....
gi 119625123  160 VTGSGHVSVPFPDT 173
Cdd:pfam04573 159 GETAGSSSFTFPDE 172
 
Name Accession Description Interval E-value
SPC22 pfam04573
Signal peptidase subunit; Translocation of polypeptide chains across the endoplasmic reticulum ...
 1-173 4.16e-79

Signal peptidase subunit; Translocation of polypeptide chains across the endoplasmic reticulum membrane is triggered by signal sequences. During translocation of the nascent chain through the membrane, the signal sequence of most secretory and membrane proteins is cleaved off. Cleavage occurs by the signal peptidase complex (SPC) which consists of four subunits in yeast and five in mammals. This family is common to yeast and mammals.


Pssm-ID: 461357  Cd Length: 172  Bit Score: 232.84  E-value: 4.16e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625123    1 MNTVLSRANSLFAFSLSVMAALTFGCFITTAFKDRSvPVRLHVSRIMLKNVEDFTGPR-ERSDLGFITFDITADIQNIFD 79
Cdd:pfam04573   1 MHSLLQRLNAVSAFALTVLAVLCALIALSSLFQDTS-SISNIVPSVKVKNSRYYGSVRgKPKDNAKITFDLDADLSPLFN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625123   80 WNVKQLFLYLSAEYSTKNNALNQVVLWDKIVLRGDNPKLLLKDMKTKYFFFDDGNGLKGnRNVTLTLSWNVVPNAGILPL 159
Cdd:pfam04573  80 WNTKQLFVYLTAEYETKKNSVNQVVIWDKIIRSKEDAKLNLKNAKSKYSFWDDGNSLRG-RNVTLTLHWNVMPWVGLLPY 158

                         170
                  ....*....|....
gi 119625123  160 VTGSGHVSVPFPDT 173
Cdd:pfam04573 159 GETAGSSSFTFPDE 172
PTZ00116 PTZ00116
signal peptidase; Provisional
 1-174 8.11e-14

signal peptidase; Provisional


Pssm-ID: 173408  Cd Length: 185  Bit Score: 66.23  E-value: 8.11e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625123   1 MNTVLSRANSLF---AFSLSVMAALTFGCFITTaFKDRSVPvrlhvSRIMLKNVEDFTGPRE-RSDLGFITFDITADIQN 76
Cdd:PTZ00116   1 MDNVLNRLNVLSysmALCFLILCLFNYGTSFYL-FDEKEMS-----TNIKVKSVKRLVYNRHiKGDEAVLSLDLSYDMSK 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625123  77 IFDWNVKQLFLYLSAEYSTKNNALNQVVLWDKIVLRGDNPKLLLKDMKTKYFFFDDGNGLKgNRNVTLTLSWNVVPNAGI 156
Cdd:PTZ00116  75 AFNWNLKQLFLYVLVTYETPEKVKNEVIIQDYIITNKKQAKKTYKNFITKYSLKDYNNGLR-NNNINLQVCYKYMPIVGL 153

                        170
                 ....*....|....*...
gi 119625123 157 LPLVTGSgHVSVPFPDTY 174
Cdd:PTZ00116 154 SRSYEGA-KISYKLPAEY 170
 
Name Accession Description Interval E-value
SPC22 pfam04573
Signal peptidase subunit; Translocation of polypeptide chains across the endoplasmic reticulum ...
 1-173 4.16e-79

Signal peptidase subunit; Translocation of polypeptide chains across the endoplasmic reticulum membrane is triggered by signal sequences. During translocation of the nascent chain through the membrane, the signal sequence of most secretory and membrane proteins is cleaved off. Cleavage occurs by the signal peptidase complex (SPC) which consists of four subunits in yeast and five in mammals. This family is common to yeast and mammals.


Pssm-ID: 461357  Cd Length: 172  Bit Score: 232.84  E-value: 4.16e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625123    1 MNTVLSRANSLFAFSLSVMAALTFGCFITTAFKDRSvPVRLHVSRIMLKNVEDFTGPR-ERSDLGFITFDITADIQNIFD 79
Cdd:pfam04573   1 MHSLLQRLNAVSAFALTVLAVLCALIALSSLFQDTS-SISNIVPSVKVKNSRYYGSVRgKPKDNAKITFDLDADLSPLFN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625123   80 WNVKQLFLYLSAEYSTKNNALNQVVLWDKIVLRGDNPKLLLKDMKTKYFFFDDGNGLKGnRNVTLTLSWNVVPNAGILPL 159
Cdd:pfam04573  80 WNTKQLFVYLTAEYETKKNSVNQVVIWDKIIRSKEDAKLNLKNAKSKYSFWDDGNSLRG-RNVTLTLHWNVMPWVGLLPY 158

                         170
                  ....*....|....
gi 119625123  160 VTGSGHVSVPFPDT 173
Cdd:pfam04573 159 GETAGSSSFTFPDE 172
PTZ00116 PTZ00116
signal peptidase; Provisional
 1-174 8.11e-14

signal peptidase; Provisional


Pssm-ID: 173408  Cd Length: 185  Bit Score: 66.23  E-value: 8.11e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625123   1 MNTVLSRANSLF---AFSLSVMAALTFGCFITTaFKDRSVPvrlhvSRIMLKNVEDFTGPRE-RSDLGFITFDITADIQN 76
Cdd:PTZ00116   1 MDNVLNRLNVLSysmALCFLILCLFNYGTSFYL-FDEKEMS-----TNIKVKSVKRLVYNRHiKGDEAVLSLDLSYDMSK 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119625123  77 IFDWNVKQLFLYLSAEYSTKNNALNQVVLWDKIVLRGDNPKLLLKDMKTKYFFFDDGNGLKgNRNVTLTLSWNVVPNAGI 156
Cdd:PTZ00116  75 AFNWNLKQLFLYVLVTYETPEKVKNEVIIQDYIITNKKQAKKTYKNFITKYSLKDYNNGLR-NNNINLQVCYKYMPIVGL 153

                        170
                 ....*....|....*...
gi 119625123 157 LPLVTGSgHVSVPFPDTY 174
Cdd:PTZ00116 154 SRSYEGA-KISYKLPAEY 170
 
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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