NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|489175445|ref|WP_003084971|]
View 

MULTISPECIES: M48 family metallopeptidase [Pseudomonas]

Protein Classification

M48 family metallopeptidase( domain architecture ID 11574951)

M48 family metallopeptidase, a member of a zinc metalloprotease family, which typically contains an HExxH motif characteristic of zinc metallopeptidases, and proteolytically removes the C-terminal three residues of farnesylated proteins

EC:  3.4.24.-
MEROPS:  M48
PubMed:  7674922|10493853

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
M48_yhfN_like cd07344
Peptidase M48 YhfN-like, a novel minigluzincin; M48 YhfN-like protease is considered as a CaaX ...
110-150 5.99e-10

Peptidase M48 YhfN-like, a novel minigluzincin; M48 YhfN-like protease is considered as a CaaX prenyl protease 1 homolog, with most of the sequences in this family as yet uncharacterized. It contains the zinc metalloprotease motif (HEXXH), likely exposed on the cytoplasmic side. It is probably associated with the endoplasmic reticulum (ER), regardless of whether its genes possess the conventional signal motif (KKXX) in the C-terminal. Proteins in this family proteolytically remove the C-terminal three residues of farnesylated proteins. This novel family of related proteins consist of the soluble minimal scaffold similar to the catalytic domains of the integral-membrane metallopeptidase M48 and M56, thus called minigluzincins.


:

Pssm-ID: 320703  Cd Length: 96  Bit Score: 53.22  E-value: 5.99e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 489175445 110 AAPEFLRMIVVHELAHLKESEHNKAFYQLCQYMLPDYHQLE 150
Cdd:cd07344   50 APPEVIDYVVVHELAHLKHMNHSPRFWALVERYMPDYKERR 90
 
Name Accession Description Interval E-value
M48_yhfN_like cd07344
Peptidase M48 YhfN-like, a novel minigluzincin; M48 YhfN-like protease is considered as a CaaX ...
110-150 5.99e-10

Peptidase M48 YhfN-like, a novel minigluzincin; M48 YhfN-like protease is considered as a CaaX prenyl protease 1 homolog, with most of the sequences in this family as yet uncharacterized. It contains the zinc metalloprotease motif (HEXXH), likely exposed on the cytoplasmic side. It is probably associated with the endoplasmic reticulum (ER), regardless of whether its genes possess the conventional signal motif (KKXX) in the C-terminal. Proteins in this family proteolytically remove the C-terminal three residues of farnesylated proteins. This novel family of related proteins consist of the soluble minimal scaffold similar to the catalytic domains of the integral-membrane metallopeptidase M48 and M56, thus called minigluzincins.


Pssm-ID: 320703  Cd Length: 96  Bit Score: 53.22  E-value: 5.99e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 489175445 110 AAPEFLRMIVVHELAHLKESEHNKAFYQLCQYMLPDYHQLE 150
Cdd:cd07344   50 APPEVIDYVVVHELAHLKHMNHSPRFWALVERYMPDYKERR 90
YgjP COG1451
UTP pyrophosphatase, metal-dependent hydrolase family [General function prediction only];
110-156 4.66e-09

UTP pyrophosphatase, metal-dependent hydrolase family [General function prediction only];


Pssm-ID: 441060  Cd Length: 236  Bit Score: 53.35  E-value: 4.66e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 489175445 110 AAPEFLRMIVVHELAHLKESEHNKAFYQLCQYMLPDYHQLEFDLRVY 156
Cdd:COG1451  184 APPEVIDYVVVHELAHLREMNHSPRFWALVERLMPDYRERRKWLKEN 230
YgjP-like pfam01863
YgjP-like, metallopeptidase domain; This is a conserved domain containing the catalytic ...
110-146 1.17e-08

YgjP-like, metallopeptidase domain; This is a conserved domain containing the catalytic zinc-metallopeptidase (HExxH) catalytic motif. Proteins containing this domain are found in some archaebacteria, as well as Helicobacter pylori. The proteins are 190-240 amino acids long, with the C terminus being the most conserved region, containing three conserved histidines. This domain is found in YgjP from E. coli, a predicted metal-dependent hydrolase that hydrolyses UTP to UMP and diphosphate in vitro; and in MJ0123 from Methanocaldococcus jannaschii (also referred to as projannalysin).


Pssm-ID: 396437  Cd Length: 207  Bit Score: 51.91  E-value: 1.17e-08
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 489175445  110 AAPEFLRMIVVHELAHLKESEHNKAFYQLCQYMLPDY 146
Cdd:pfam01863 161 APPECIDYVVVHELCHLLEPNHSPRFWALVERYMPDW 197
 
Name Accession Description Interval E-value
M48_yhfN_like cd07344
Peptidase M48 YhfN-like, a novel minigluzincin; M48 YhfN-like protease is considered as a CaaX ...
110-150 5.99e-10

Peptidase M48 YhfN-like, a novel minigluzincin; M48 YhfN-like protease is considered as a CaaX prenyl protease 1 homolog, with most of the sequences in this family as yet uncharacterized. It contains the zinc metalloprotease motif (HEXXH), likely exposed on the cytoplasmic side. It is probably associated with the endoplasmic reticulum (ER), regardless of whether its genes possess the conventional signal motif (KKXX) in the C-terminal. Proteins in this family proteolytically remove the C-terminal three residues of farnesylated proteins. This novel family of related proteins consist of the soluble minimal scaffold similar to the catalytic domains of the integral-membrane metallopeptidase M48 and M56, thus called minigluzincins.


Pssm-ID: 320703  Cd Length: 96  Bit Score: 53.22  E-value: 5.99e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 489175445 110 AAPEFLRMIVVHELAHLKESEHNKAFYQLCQYMLPDYHQLE 150
Cdd:cd07344   50 APPEVIDYVVVHELAHLKHMNHSPRFWALVERYMPDYKERR 90
YgjP COG1451
UTP pyrophosphatase, metal-dependent hydrolase family [General function prediction only];
110-156 4.66e-09

UTP pyrophosphatase, metal-dependent hydrolase family [General function prediction only];


Pssm-ID: 441060  Cd Length: 236  Bit Score: 53.35  E-value: 4.66e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 489175445 110 AAPEFLRMIVVHELAHLKESEHNKAFYQLCQYMLPDYHQLEFDLRVY 156
Cdd:COG1451  184 APPEVIDYVVVHELAHLREMNHSPRFWALVERLMPDYRERRKWLKEN 230
YgjP-like pfam01863
YgjP-like, metallopeptidase domain; This is a conserved domain containing the catalytic ...
110-146 1.17e-08

YgjP-like, metallopeptidase domain; This is a conserved domain containing the catalytic zinc-metallopeptidase (HExxH) catalytic motif. Proteins containing this domain are found in some archaebacteria, as well as Helicobacter pylori. The proteins are 190-240 amino acids long, with the C terminus being the most conserved region, containing three conserved histidines. This domain is found in YgjP from E. coli, a predicted metal-dependent hydrolase that hydrolyses UTP to UMP and diphosphate in vitro; and in MJ0123 from Methanocaldococcus jannaschii (also referred to as projannalysin).


Pssm-ID: 396437  Cd Length: 207  Bit Score: 51.91  E-value: 1.17e-08
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 489175445  110 AAPEFLRMIVVHELAHLKESEHNKAFYQLCQYMLPDY 146
Cdd:pfam01863 161 APPECIDYVVVHELCHLLEPNHSPRFWALVERYMPDW 197
 
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