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Conserved domains on  [gi|344233686|gb|EGV65558|]
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signal peptidase 22 kDa subunit [Yamadazyma tenuis ATCC 10573]

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 ...
 1-182 1.01e-86

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: 252.48  E-value: 1.01e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344233686    1 MFNLVTRAQAISNHAITCTAIIAALVIVSSFFQlqldqvwslNTTSISNVQAGASLKGSFQYGAKNGKQKENSIIKFDLD 80
Cdd:pfam04573   1 MHSLLQRLNAVSAFALTVLAVLCALIALSSLFQ---------DTSSISNIVPSVKVKNSRYYGSVRGKPKDNAKITFDLD 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344233686   81 ADLTPLFNWNTKQVFVYLTAEYPGKSdGSSNKVTYWDKIITSKDDAVLSLKNHRAKYSVWDVENSFRQRDAELKLEWNIQ 160
Cdd:pfam04573  72 ADLSPLFNWNTKQLFVYLTAEYETKK-NSVNQVVIWDKIIRSKEDAKLNLKNAKSKYSFWDDGNSLRGRNVTLTLHWNVM 150

                         170       180
                  ....*....|....*....|..
gi 344233686  161 PHVGPLIFGQTSATTPFTFAEV 182
Cdd:pfam04573 151 PWVGLLPYGETAGSSSFTFPDE 172
 
Name Accession Description Interval E-value
SPC22 pfam04573
Signal peptidase subunit; Translocation of polypeptide chains across the endoplasmic reticulum ...
 1-182 1.01e-86

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: 252.48  E-value: 1.01e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344233686    1 MFNLVTRAQAISNHAITCTAIIAALVIVSSFFQlqldqvwslNTTSISNVQAGASLKGSFQYGAKNGKQKENSIIKFDLD 80
Cdd:pfam04573   1 MHSLLQRLNAVSAFALTVLAVLCALIALSSLFQ---------DTSSISNIVPSVKVKNSRYYGSVRGKPKDNAKITFDLD 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344233686   81 ADLTPLFNWNTKQVFVYLTAEYPGKSdGSSNKVTYWDKIITSKDDAVLSLKNHRAKYSVWDVENSFRQRDAELKLEWNIQ 160
Cdd:pfam04573  72 ADLSPLFNWNTKQLFVYLTAEYETKK-NSVNQVVIWDKIIRSKEDAKLNLKNAKSKYSFWDDGNSLRGRNVTLTLHWNVM 150

                         170       180
                  ....*....|....*....|..
gi 344233686  161 PHVGPLIFGQTSATTPFTFAEV 182
Cdd:pfam04573 151 PWVGLLPYGETAGSSSFTFPDE 172
PTZ00116 PTZ00116
signal peptidase; Provisional
 1-164 1.62e-11

signal peptidase; Provisional


Pssm-ID: 173408  Cd Length: 185  Bit Score: 60.06  E-value: 1.62e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344233686   1 MFNLVTRAQAISNHAITCTAIIAALVIVSSFFQLQLDQV-WSLNTTSISNVQAGASLKGsfqygakngkqkENSIIKFDL 79
Cdd:PTZ00116   1 MDNVLNRLNVLSYSMALCFLILCLFNYGTSFYLFDEKEMsTNIKVKSVKRLVYNRHIKG------------DEAVLSLDL 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344233686  80 DADLTPLFNWNTKQVFVY--LTAEYPGKsdgSSNKVTYWDKIITSKDDAVLSLKNHRAKYSVWDVENSFRQRDAELKLEW 157
Cdd:PTZ00116  69 SYDMSKAFNWNLKQLFLYvlVTYETPEK---VKNEVIIQDYIITNKKQAKKTYKNFITKYSLKDYNNGLRNNNINLQVCY 145


                 ....*..
gi 344233686 158 NIQPHVG 164
Cdd:PTZ00116 146 KYMPIVG 152
 
Name Accession Description Interval E-value
SPC22 pfam04573
Signal peptidase subunit; Translocation of polypeptide chains across the endoplasmic reticulum ...
 1-182 1.01e-86

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: 252.48  E-value: 1.01e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344233686    1 MFNLVTRAQAISNHAITCTAIIAALVIVSSFFQlqldqvwslNTTSISNVQAGASLKGSFQYGAKNGKQKENSIIKFDLD 80
Cdd:pfam04573   1 MHSLLQRLNAVSAFALTVLAVLCALIALSSLFQ---------DTSSISNIVPSVKVKNSRYYGSVRGKPKDNAKITFDLD 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344233686   81 ADLTPLFNWNTKQVFVYLTAEYPGKSdGSSNKVTYWDKIITSKDDAVLSLKNHRAKYSVWDVENSFRQRDAELKLEWNIQ 160
Cdd:pfam04573  72 ADLSPLFNWNTKQLFVYLTAEYETKK-NSVNQVVIWDKIIRSKEDAKLNLKNAKSKYSFWDDGNSLRGRNVTLTLHWNVM 150

                         170       180
                  ....*....|....*....|..
gi 344233686  161 PHVGPLIFGQTSATTPFTFAEV 182
Cdd:pfam04573 151 PWVGLLPYGETAGSSSFTFPDE 172
PTZ00116 PTZ00116
signal peptidase; Provisional
 1-164 1.62e-11

signal peptidase; Provisional


Pssm-ID: 173408  Cd Length: 185  Bit Score: 60.06  E-value: 1.62e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344233686   1 MFNLVTRAQAISNHAITCTAIIAALVIVSSFFQLQLDQV-WSLNTTSISNVQAGASLKGsfqygakngkqkENSIIKFDL 79
Cdd:PTZ00116   1 MDNVLNRLNVLSYSMALCFLILCLFNYGTSFYLFDEKEMsTNIKVKSVKRLVYNRHIKG------------DEAVLSLDL 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344233686  80 DADLTPLFNWNTKQVFVY--LTAEYPGKsdgSSNKVTYWDKIITSKDDAVLSLKNHRAKYSVWDVENSFRQRDAELKLEW 157
Cdd:PTZ00116  69 SYDMSKAFNWNLKQLFLYvlVTYETPEK---VKNEVIIQDYIITNKKQAKKTYKNFITKYSLKDYNNGLRNNNINLQVCY 145


                 ....*..
gi 344233686 158 NIQPHVG 164
Cdd:PTZ00116 146 KYMPIVG 152
 
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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