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Conserved domains on  [gi|162417971|ref|NP_055567|]
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signal peptidase complex subunit 2 [Homo sapiens]

Protein Classification

signal peptidase complex subunit 2( domain architecture ID 10535464)

signal peptidase complex subunit 2 is a component of the microsomal signal peptidase complex which removes signal peptides from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum

PubMed:  8632014

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SPC25 pfam06703
Microsomal signal peptidase 25 kDa subunit (SPC25); This family consists of several microsomal ...
61-217 3.51e-56

Microsomal signal peptidase 25 kDa subunit (SPC25); This family consists of several microsomal signal peptidase 25 kDa subunit proteins. Translocation of polypeptide chains across the endoplasmic reticulum (ER) membrane is triggered by signal sequences. Subsequently, signal recognition particle interacts with its membrane receptor and the ribosome-bound nascent chain is targeted to the ER where it is transferred into a protein-conducting channel. At some point, a second signal sequence recognition event takes place in the membrane and translocation of the nascent chain through the membrane occurs. The signal sequence of most secretory and membrane proteins is cleaved off at this stage. Cleavage occurs by the signal peptidase complex (SPC) as soon as the lumenal domain of the translocating polypeptide is large enough to expose its cleavage site to the enzyme. The signal peptidase complex is possibly also involved in proteolytic events in the ER membrane other than the processing of the signal sequence, for example the further digestion of the cleaved signal peptide or the degradation of membrane proteins. Mammalian signal peptidase is as a complex of five different polypeptide chains. This family represents the 25 kDa subunit (SPC25).


:

Pssm-ID: 461993  Cd Length: 153  Bit Score: 175.84  E-value: 3.51e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162417971   61 DDSAKKVLLEKYKYVENFGLIDGRLTICTISCFFAIVALIWDYMHPFPESKPVLALCVISYFVMMGILTIYTSYKEKSIF 140
Cdd:pfam06703   1 DDALPEYLTSLKGYKESHTLTDVRLALGYLAVAIAAAAFLYDYKFGFPESKPYLIVCVALYFILSGILTLWTKFVEKGIV 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 162417971  141 LVAHRKDPTGmdpddIWQLSSSLKRFDDKYTLKLTFISGRTKQQ-REAEFTKSIAKFFDHSGTLVMDAYEPEISRLHD 217
Cdd:pfam06703  81 YVGTRKDGSG-----KITISSSLKKYDPIYTLTITYKDTSKGGKsLKKELEKPVTKWFDEDGYLVEDLFEKWLAKLLE 153
 
Name Accession Description Interval E-value
SPC25 pfam06703
Microsomal signal peptidase 25 kDa subunit (SPC25); This family consists of several microsomal ...
61-217 3.51e-56

Microsomal signal peptidase 25 kDa subunit (SPC25); This family consists of several microsomal signal peptidase 25 kDa subunit proteins. Translocation of polypeptide chains across the endoplasmic reticulum (ER) membrane is triggered by signal sequences. Subsequently, signal recognition particle interacts with its membrane receptor and the ribosome-bound nascent chain is targeted to the ER where it is transferred into a protein-conducting channel. At some point, a second signal sequence recognition event takes place in the membrane and translocation of the nascent chain through the membrane occurs. The signal sequence of most secretory and membrane proteins is cleaved off at this stage. Cleavage occurs by the signal peptidase complex (SPC) as soon as the lumenal domain of the translocating polypeptide is large enough to expose its cleavage site to the enzyme. The signal peptidase complex is possibly also involved in proteolytic events in the ER membrane other than the processing of the signal sequence, for example the further digestion of the cleaved signal peptide or the degradation of membrane proteins. Mammalian signal peptidase is as a complex of five different polypeptide chains. This family represents the 25 kDa subunit (SPC25).


Pssm-ID: 461993  Cd Length: 153  Bit Score: 175.84  E-value: 3.51e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162417971   61 DDSAKKVLLEKYKYVENFGLIDGRLTICTISCFFAIVALIWDYMHPFPESKPVLALCVISYFVMMGILTIYTSYKEKSIF 140
Cdd:pfam06703   1 DDALPEYLTSLKGYKESHTLTDVRLALGYLAVAIAAAAFLYDYKFGFPESKPYLIVCVALYFILSGILTLWTKFVEKGIV 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 162417971  141 LVAHRKDPTGmdpddIWQLSSSLKRFDDKYTLKLTFISGRTKQQ-REAEFTKSIAKFFDHSGTLVMDAYEPEISRLHD 217
Cdd:pfam06703  81 YVGTRKDGSG-----KITISSSLKKYDPIYTLTITYKDTSKGGKsLKKELEKPVTKWFDEDGYLVEDLFEKWLAKLLE 153
 
Name Accession Description Interval E-value
SPC25 pfam06703
Microsomal signal peptidase 25 kDa subunit (SPC25); This family consists of several microsomal ...
61-217 3.51e-56

Microsomal signal peptidase 25 kDa subunit (SPC25); This family consists of several microsomal signal peptidase 25 kDa subunit proteins. Translocation of polypeptide chains across the endoplasmic reticulum (ER) membrane is triggered by signal sequences. Subsequently, signal recognition particle interacts with its membrane receptor and the ribosome-bound nascent chain is targeted to the ER where it is transferred into a protein-conducting channel. At some point, a second signal sequence recognition event takes place in the membrane and translocation of the nascent chain through the membrane occurs. The signal sequence of most secretory and membrane proteins is cleaved off at this stage. Cleavage occurs by the signal peptidase complex (SPC) as soon as the lumenal domain of the translocating polypeptide is large enough to expose its cleavage site to the enzyme. The signal peptidase complex is possibly also involved in proteolytic events in the ER membrane other than the processing of the signal sequence, for example the further digestion of the cleaved signal peptide or the degradation of membrane proteins. Mammalian signal peptidase is as a complex of five different polypeptide chains. This family represents the 25 kDa subunit (SPC25).


Pssm-ID: 461993  Cd Length: 153  Bit Score: 175.84  E-value: 3.51e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162417971   61 DDSAKKVLLEKYKYVENFGLIDGRLTICTISCFFAIVALIWDYMHPFPESKPVLALCVISYFVMMGILTIYTSYKEKSIF 140
Cdd:pfam06703   1 DDALPEYLTSLKGYKESHTLTDVRLALGYLAVAIAAAAFLYDYKFGFPESKPYLIVCVALYFILSGILTLWTKFVEKGIV 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 162417971  141 LVAHRKDPTGmdpddIWQLSSSLKRFDDKYTLKLTFISGRTKQQ-REAEFTKSIAKFFDHSGTLVMDAYEPEISRLHD 217
Cdd:pfam06703  81 YVGTRKDGSG-----KITISSSLKKYDPIYTLTITYKDTSKGGKsLKKELEKPVTKWFDEDGYLVEDLFEKWLAKLLE 153
 
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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