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Conserved domains on  [gi|21355207|ref|NP_651234|]
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spase 22/23-subunit, isoform A [Drosophila melanogaster]

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 ...
 1-172 3.68e-80

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: 235.15  E-value: 3.68e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355207     1 MHTVLTRGNATVAYTLSVLACLTFSCFLSTVFLDyRTDANINTVRVLVKNVPDYGASR-EKHDLGFVTFDLQTNLTGIFN 79
Cdd:pfam04573   1 MHSLLQRLNAVSAFALTVLAVLCALIALSSLFQD-TSSISNIVPSVKVKNSRYYGSVRgKPKDNAKITFDLDADLSPLFN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355207    80 WNVKQLFLYLTAEYQTPANQLNQVVLWDKIILRGDNAVLDFKNMNTKYYFWDDGNGLKdNRNVSLYLSWNIIPNAGLLPS 159
Cdd:pfam04573  80 WNTKQLFVYLTAEYETKKNSVNQVVIWDKIIRSKEDAKLNLKNAKSKYSFWDDGNSLR-GRNVTLTLHWNVMPWVGLLPY 158

                         170
                  ....*....|...
gi 21355207   160 VQATGKHLFKFPA 172
Cdd:pfam04573 159 GETAGSSSFTFPD 171
 
Name Accession Description Interval E-value
SPC22 pfam04573
Signal peptidase subunit; Translocation of polypeptide chains across the endoplasmic reticulum ...
 1-172 3.68e-80

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: 235.15  E-value: 3.68e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355207     1 MHTVLTRGNATVAYTLSVLACLTFSCFLSTVFLDyRTDANINTVRVLVKNVPDYGASR-EKHDLGFVTFDLQTNLTGIFN 79
Cdd:pfam04573   1 MHSLLQRLNAVSAFALTVLAVLCALIALSSLFQD-TSSISNIVPSVKVKNSRYYGSVRgKPKDNAKITFDLDADLSPLFN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355207    80 WNVKQLFLYLTAEYQTPANQLNQVVLWDKIILRGDNAVLDFKNMNTKYYFWDDGNGLKdNRNVSLYLSWNIIPNAGLLPS 159
Cdd:pfam04573  80 WNTKQLFVYLTAEYETKKNSVNQVVIWDKIIRSKEDAKLNLKNAKSKYSFWDDGNSLR-GRNVTLTLHWNVMPWVGLLPY 158

                         170
                  ....*....|...
gi 21355207   160 VQATGKHLFKFPA 172
Cdd:pfam04573 159 GETAGSSSFTFPD 171
PTZ00116 PTZ00116
signal peptidase; Provisional
 1-174 8.36e-19

signal peptidase; Provisional


Pssm-ID: 173408  Cd Length: 185  Bit Score: 79.32  E-value: 8.36e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355207    1 MHTVLTRGNaTVAYTLSVlacltfsCFLSTVFLDYRT-----DANINTVRVLVKNVPDYGASRE-KHDLGFVTFDLQTNL 74
Cdd:PTZ00116   1 MDNVLNRLN-VLSYSMAL-------CFLILCLFNYGTsfylfDEKEMSTNIKVKSVKRLVYNRHiKGDEAVLSLDLSYDM 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355207   75 TGIFNWNVKQLFLYLTAEYQTPANQLNQVVLWDKIILRGDNAVLDFKNMNTKYYFWDDGNGLKDNrNVSLYLSWNIIPNA 154
Cdd:PTZ00116  73 SKAFNWNLKQLFLYVLVTYETPEKVKNEVIIQDYIITNKKQAKKTYKNFITKYSLKDYNNGLRNN-NINLQVCYKYMPIV 151

                        170       180
                 ....*....|....*....|
gi 21355207  155 GLLPSVQATgKHLFKFPADY 174
Cdd:PTZ00116 152 GLSRSYEGA-KISYKLPAEY 170
 
Name Accession Description Interval E-value
SPC22 pfam04573
Signal peptidase subunit; Translocation of polypeptide chains across the endoplasmic reticulum ...
 1-172 3.68e-80

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: 235.15  E-value: 3.68e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355207     1 MHTVLTRGNATVAYTLSVLACLTFSCFLSTVFLDyRTDANINTVRVLVKNVPDYGASR-EKHDLGFVTFDLQTNLTGIFN 79
Cdd:pfam04573   1 MHSLLQRLNAVSAFALTVLAVLCALIALSSLFQD-TSSISNIVPSVKVKNSRYYGSVRgKPKDNAKITFDLDADLSPLFN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355207    80 WNVKQLFLYLTAEYQTPANQLNQVVLWDKIILRGDNAVLDFKNMNTKYYFWDDGNGLKdNRNVSLYLSWNIIPNAGLLPS 159
Cdd:pfam04573  80 WNTKQLFVYLTAEYETKKNSVNQVVIWDKIIRSKEDAKLNLKNAKSKYSFWDDGNSLR-GRNVTLTLHWNVMPWVGLLPY 158

                         170
                  ....*....|...
gi 21355207   160 VQATGKHLFKFPA 172
Cdd:pfam04573 159 GETAGSSSFTFPD 171
PTZ00116 PTZ00116
signal peptidase; Provisional
 1-174 8.36e-19

signal peptidase; Provisional


Pssm-ID: 173408  Cd Length: 185  Bit Score: 79.32  E-value: 8.36e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355207    1 MHTVLTRGNaTVAYTLSVlacltfsCFLSTVFLDYRT-----DANINTVRVLVKNVPDYGASRE-KHDLGFVTFDLQTNL 74
Cdd:PTZ00116   1 MDNVLNRLN-VLSYSMAL-------CFLILCLFNYGTsfylfDEKEMSTNIKVKSVKRLVYNRHiKGDEAVLSLDLSYDM 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355207   75 TGIFNWNVKQLFLYLTAEYQTPANQLNQVVLWDKIILRGDNAVLDFKNMNTKYYFWDDGNGLKDNrNVSLYLSWNIIPNA 154
Cdd:PTZ00116  73 SKAFNWNLKQLFLYVLVTYETPEKVKNEVIIQDYIITNKKQAKKTYKNFITKYSLKDYNNGLRNN-NINLQVCYKYMPIV 151

                        170       180
                 ....*....|....*....|
gi 21355207  155 GLLPSVQATgKHLFKFPADY 174
Cdd:PTZ00116 152 GLSRSYEGA-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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