NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1179975816|ref|WP_083498170|]
View 

A24 family peptidase [Staphylococcus auricularis]

Protein Classification

prepilin peptidase( domain architecture ID 11449472)

prepilin peptidase, A24 family peptidase, processes type 4 pilin precursor proteins (prepilins) to their mature forms by removal of leader peptides

CATH:  1.20.120.1220
EC:  3.4.23.43
Gene Ontology:  GO:0004190|GO:0016020
MEROPS:  A24
PubMed:  25793961|7961448

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PulO COG1989
Prepilin signal peptidase PulO (type II secretory pathway) or related peptidase [Cell motility, ...
 31-223 2.61e-27

Prepilin signal peptidase PulO (type II secretory pathway) or related peptidase [Cell motility, Intracellular trafficking, secretion, and vesicular transport];


:

Pssm-ID: 441592 [Multi-domain]  Cd Length: 256  Bit Score: 104.87  E-value: 2.61e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179975816  31 LYSRSRCDYCHRSLSTLELIPIISYLIQKGRSRCCHQKLSMLYPLGEIIS--LSAIPLLNMSLPITSELFLLLFFLLLTL 108
Cdd:COG1989    35 VFPRSHCPHCGHPLRWYDNIPVLSYLLLRGRCRYCGAPISLRYPLVELLTglLFLLLALRFGLSLQLLAALLLLSLLLAL 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179975816 109 SIFDMATLSIPLHMMIIFSCCCYFYSDIH--------LTHAFFMIIGLHLFYFC-----SRRAMGYGDILVFSMLACFLP 175
Cdd:COG1989   115 SFIDLDTQLLPDSLTLPLLWLGLLLSLLGgfvslldaLLGALAGYLLLWLIYWLfklltGKEGMGGGDVKLLAALGAWLG 194

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1179975816 176 IIVFIYVFLFTFIIGGIVMLSIMLYKRQRLTHHVPLVPFIFLSFCFVI 223
Cdd:COG1989   195 WQALLLILLLASLLGALVGLILLLLGRKGRKTPIPFGPFLALGGLIAL 242
 
Name Accession Description Interval E-value
PulO COG1989
Prepilin signal peptidase PulO (type II secretory pathway) or related peptidase [Cell motility, ...
 31-223 2.61e-27

Prepilin signal peptidase PulO (type II secretory pathway) or related peptidase [Cell motility, Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 441592 [Multi-domain]  Cd Length: 256  Bit Score: 104.87  E-value: 2.61e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179975816  31 LYSRSRCDYCHRSLSTLELIPIISYLIQKGRSRCCHQKLSMLYPLGEIIS--LSAIPLLNMSLPITSELFLLLFFLLLTL 108
Cdd:COG1989    35 VFPRSHCPHCGHPLRWYDNIPVLSYLLLRGRCRYCGAPISLRYPLVELLTglLFLLLALRFGLSLQLLAALLLLSLLLAL 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179975816 109 SIFDMATLSIPLHMMIIFSCCCYFYSDIH--------LTHAFFMIIGLHLFYFC-----SRRAMGYGDILVFSMLACFLP 175
Cdd:COG1989   115 SFIDLDTQLLPDSLTLPLLWLGLLLSLLGgfvslldaLLGALAGYLLLWLIYWLfklltGKEGMGGGDVKLLAALGAWLG 194

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1179975816 176 IIVFIYVFLFTFIIGGIVMLSIMLYKRQRLTHHVPLVPFIFLSFCFVI 223
Cdd:COG1989   195 WQALLLILLLASLLGALVGLILLLLGRKGRKTPIPFGPFLALGGLIAL 242
DiS_P_DiS pfam06750
Bacterial Peptidase A24 N-terminal domain; This family is found at the N-terminus of the ...
 31-80 3.26e-14

Bacterial Peptidase A24 N-terminal domain; This family is found at the N-terminus of the pre-pilin peptidases (pfam01478). It's function has not been specifically determined; however some of the family have been characterized as bifunctional, and this domain may contain the N-methylation activity (EC:2.1.1.-). It consists of an intracellular region between a pair of transmembrane. This region contains an invariant proline and two almost fully conserved disulphide bridges - hence the name DiS-P-DiS. The cysteines have been shown to be essential to the overall function of the enzyme in, but their role was incorrectly ascribed.


Pssm-ID: 462001  Cd Length: 84  Bit Score: 65.54  E-value: 3.26e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1179975816  31 LYSRSRCDYCHRSLSTLELIPIISYLIQKGRSRCCHQKLSMLYPLGEIIS 80
Cdd:pfam06750  24 VFPRSHCPSCGHRLRWYDNIPVLSWLLLRGRCRYCGAKISIRYPLVELLT 73
 
Name Accession Description Interval E-value
PulO COG1989
Prepilin signal peptidase PulO (type II secretory pathway) or related peptidase [Cell motility, ...
 31-223 2.61e-27

Prepilin signal peptidase PulO (type II secretory pathway) or related peptidase [Cell motility, Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 441592 [Multi-domain]  Cd Length: 256  Bit Score: 104.87  E-value: 2.61e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179975816  31 LYSRSRCDYCHRSLSTLELIPIISYLIQKGRSRCCHQKLSMLYPLGEIIS--LSAIPLLNMSLPITSELFLLLFFLLLTL 108
Cdd:COG1989    35 VFPRSHCPHCGHPLRWYDNIPVLSYLLLRGRCRYCGAPISLRYPLVELLTglLFLLLALRFGLSLQLLAALLLLSLLLAL 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179975816 109 SIFDMATLSIPLHMMIIFSCCCYFYSDIH--------LTHAFFMIIGLHLFYFC-----SRRAMGYGDILVFSMLACFLP 175
Cdd:COG1989   115 SFIDLDTQLLPDSLTLPLLWLGLLLSLLGgfvslldaLLGALAGYLLLWLIYWLfklltGKEGMGGGDVKLLAALGAWLG 194

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1179975816 176 IIVFIYVFLFTFIIGGIVMLSIMLYKRQRLTHHVPLVPFIFLSFCFVI 223
Cdd:COG1989   195 WQALLLILLLASLLGALVGLILLLLGRKGRKTPIPFGPFLALGGLIAL 242
DiS_P_DiS pfam06750
Bacterial Peptidase A24 N-terminal domain; This family is found at the N-terminus of the ...
 31-80 3.26e-14

Bacterial Peptidase A24 N-terminal domain; This family is found at the N-terminus of the pre-pilin peptidases (pfam01478). It's function has not been specifically determined; however some of the family have been characterized as bifunctional, and this domain may contain the N-methylation activity (EC:2.1.1.-). It consists of an intracellular region between a pair of transmembrane. This region contains an invariant proline and two almost fully conserved disulphide bridges - hence the name DiS-P-DiS. The cysteines have been shown to be essential to the overall function of the enzyme in, but their role was incorrectly ascribed.


Pssm-ID: 462001  Cd Length: 84  Bit Score: 65.54  E-value: 3.26e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1179975816  31 LYSRSRCDYCHRSLSTLELIPIISYLIQKGRSRCCHQKLSMLYPLGEIIS 80
Cdd:pfam06750  24 VFPRSHCPSCGHRLRWYDNIPVLSWLLLRGRCRYCGAKISIRYPLVELLT 73
CpaA COG4960
Flp pilus assembly protein, peptidase CpaA [Posttranslational modification, protein turnover, ...
 138-213 4.32e-03

Flp pilus assembly protein, peptidase CpaA [Posttranslational modification, protein turnover, chaperones, Signal transduction mechanisms];


Pssm-ID: 443986  Cd Length: 161  Bit Score: 36.79  E-value: 4.32e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1179975816 138 LTHAFFMIIGLHLFYFC-SRRAMGYGDILVFSMLACFLPIIVFIYVFLFTFIIGGIVMLSIMLYKRQRLTHHVPLVP 213
Cdd:COG4960    55 GLSLLGALIGLAVGFPLfALGGMGGGDVKLLAALGLWLGPAALLLFLLLTALAGGVLALILLLLRRLPAAAGRPPWL 131
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH