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Conserved domains on  [gi|493494014|ref|WP_006448660|]
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SprT family zinc-dependent metalloprotease [Xanthomonas hortorum]

Protein Classification

SprT family zinc-dependent metalloprotease( domain architecture ID 10486918)

SprT family zinc-dependent metalloprotease, which contains an HExxH motif characteristic of zinc metallopeptidases

CATH:  3.30.2010.10
EC:  3.4.-.-
Gene Ontology:  GO:0008237|GO:0006508|GO:0046872

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YgjP-like pfam01863
YgjP-like, metallopeptidase domain; This is a conserved domain containing the catalytic ...
 33-239 3.33e-70

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: 214.08  E-value: 3.33e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493494014   33 RVAIHVEPDGRVRLDAPLQATDAQIKRALIQRARWIHLHLMEIEQRlRHVTPREYVSGETVLYLGRRYRLKVILGDQIQG 112
Cdd:pfam01863   2 NLRLRVEPDGGVRVSAPLGVPEEEIEDFLQKKADWILKKLARFEEL-ARPAEREYVSGESFPLLGRPYRLKVIPGKRLSV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493494014  113 VRLRGGYVEARVPSRAPEVVRAALEGWQRERARLLLPQRVADVAAQLRWikQVPPLSLRVMQRQWGSCSPLGRISLNLGL 192
Cdd:pfam01863  81 LLLRDGLLLIVLPELDPEKLRKALERWYRKRAKEILPERLARYAAKLGV--PPPSVRIRDMKTRWGSCSSKGRIRLNWRL 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 493494014  193 IRVPGACIDYVILHELCHLKVHNHGKGFYRLLDAHLPGWRGIKQRLD 239
Cdd:pfam01863 159 VKAPPECIDYVVVHELCHLLEPNHSPRFWALVERYMPDWKEAKRWLK 205
 
Name Accession Description Interval E-value
YgjP-like pfam01863
YgjP-like, metallopeptidase domain; This is a conserved domain containing the catalytic ...
 33-239 3.33e-70

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: 214.08  E-value: 3.33e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493494014   33 RVAIHVEPDGRVRLDAPLQATDAQIKRALIQRARWIHLHLMEIEQRlRHVTPREYVSGETVLYLGRRYRLKVILGDQIQG 112
Cdd:pfam01863   2 NLRLRVEPDGGVRVSAPLGVPEEEIEDFLQKKADWILKKLARFEEL-ARPAEREYVSGESFPLLGRPYRLKVIPGKRLSV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493494014  113 VRLRGGYVEARVPSRAPEVVRAALEGWQRERARLLLPQRVADVAAQLRWikQVPPLSLRVMQRQWGSCSPLGRISLNLGL 192
Cdd:pfam01863  81 LLLRDGLLLIVLPELDPEKLRKALERWYRKRAKEILPERLARYAAKLGV--PPPSVRIRDMKTRWGSCSSKGRIRLNWRL 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 493494014  193 IRVPGACIDYVILHELCHLKVHNHGKGFYRLLDAHLPGWRGIKQRLD 239
Cdd:pfam01863 159 VKAPPECIDYVVVHELCHLLEPNHSPRFWALVERYMPDWKEAKRWLK 205
YgjP COG1451
UTP pyrophosphatase, metal-dependent hydrolase family [General function prediction only];
9-239 1.85e-69

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


Pssm-ID: 441060  Cd Length: 236  Bit Score: 213.21  E-value: 1.85e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493494014   9 EMVVTYGERRIHCQIQRSALRRsqrVAIHVEPDGRVRLDAPLQATDAQIKRALIQRARWIHLHLMEIEQRLRHvTPREYV 88
Cdd:COG1451    5 TRTILLGGREIPYELRRSKRKR---LRLRVPPDGRVRVTAPLRVSLAEIEAFVRSKADWILKKLARLRERARQ-PPREFV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493494014  89 SGETVLYLGRRYRLKVILGDQiQGVRLRGGYVEARVPSRAPEVVRAALEGWQRERARLLLPQRVADVAAQLRwiKQVPPL 168
Cdd:COG1451   81 DGESLPYLGRRYRLRVVEGAR-GSVRLDGGRLLVPVPGGDPEQIRRALEDWYRRQARELLPERLARYAARLG--VKPPRV 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493494014 169 SLRVMQRQWGSCSPLGRISLNLGLIRVPGACIDYVILHELCHLKVHNHGKGFYRLLDAHLPGWRGIKQRLD 239
Cdd:COG1451  158 RIRDMKTRWGSCSSKGRIRLNWRLIMAPPEVIDYVVVHELAHLREMNHSPRFWALVERLMPDYRERRKWLK 228
M48_yhfN_like cd07344
Peptidase M48 YhfN-like, a novel minigluzincin; M48 YhfN-like protease is considered as a CaaX ...
 144-239 1.93e-34

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: 119.08  E-value: 1.93e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493494014 144 ARLLLPQRVADVAAQLRwiKQVPPLSLRVMQRQWGSCSPLGRISLNLGLIRVPGACIDYVILHELCHLKVHNHGKGFYRL 223
Cdd:cd07344    1 AKELLPERVEKYAERLG--VKPPKIRIRDMKTRWGSCSSKGNINLNWRLIKAPPEVIDYVVVHELAHLKHMNHSPRFWAL 78

                         90
                 ....*....|....*.
gi 493494014 224 LDAHLPGWRGIKQRLD 239
Cdd:cd07344   79 VERYMPDYKERRKWLK 94
 
Name Accession Description Interval E-value
YgjP-like pfam01863
YgjP-like, metallopeptidase domain; This is a conserved domain containing the catalytic ...
 33-239 3.33e-70

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: 214.08  E-value: 3.33e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493494014   33 RVAIHVEPDGRVRLDAPLQATDAQIKRALIQRARWIHLHLMEIEQRlRHVTPREYVSGETVLYLGRRYRLKVILGDQIQG 112
Cdd:pfam01863   2 NLRLRVEPDGGVRVSAPLGVPEEEIEDFLQKKADWILKKLARFEEL-ARPAEREYVSGESFPLLGRPYRLKVIPGKRLSV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493494014  113 VRLRGGYVEARVPSRAPEVVRAALEGWQRERARLLLPQRVADVAAQLRWikQVPPLSLRVMQRQWGSCSPLGRISLNLGL 192
Cdd:pfam01863  81 LLLRDGLLLIVLPELDPEKLRKALERWYRKRAKEILPERLARYAAKLGV--PPPSVRIRDMKTRWGSCSSKGRIRLNWRL 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 493494014  193 IRVPGACIDYVILHELCHLKVHNHGKGFYRLLDAHLPGWRGIKQRLD 239
Cdd:pfam01863 159 VKAPPECIDYVVVHELCHLLEPNHSPRFWALVERYMPDWKEAKRWLK 205
YgjP COG1451
UTP pyrophosphatase, metal-dependent hydrolase family [General function prediction only];
9-239 1.85e-69

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


Pssm-ID: 441060  Cd Length: 236  Bit Score: 213.21  E-value: 1.85e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493494014   9 EMVVTYGERRIHCQIQRSALRRsqrVAIHVEPDGRVRLDAPLQATDAQIKRALIQRARWIHLHLMEIEQRLRHvTPREYV 88
Cdd:COG1451    5 TRTILLGGREIPYELRRSKRKR---LRLRVPPDGRVRVTAPLRVSLAEIEAFVRSKADWILKKLARLRERARQ-PPREFV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493494014  89 SGETVLYLGRRYRLKVILGDQiQGVRLRGGYVEARVPSRAPEVVRAALEGWQRERARLLLPQRVADVAAQLRwiKQVPPL 168
Cdd:COG1451   81 DGESLPYLGRRYRLRVVEGAR-GSVRLDGGRLLVPVPGGDPEQIRRALEDWYRRQARELLPERLARYAARLG--VKPPRV 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493494014 169 SLRVMQRQWGSCSPLGRISLNLGLIRVPGACIDYVILHELCHLKVHNHGKGFYRLLDAHLPGWRGIKQRLD 239
Cdd:COG1451  158 RIRDMKTRWGSCSSKGRIRLNWRLIMAPPEVIDYVVVHELAHLREMNHSPRFWALVERLMPDYRERRKWLK 228
M48_yhfN_like cd07344
Peptidase M48 YhfN-like, a novel minigluzincin; M48 YhfN-like protease is considered as a CaaX ...
 144-239 1.93e-34

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: 119.08  E-value: 1.93e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493494014 144 ARLLLPQRVADVAAQLRwiKQVPPLSLRVMQRQWGSCSPLGRISLNLGLIRVPGACIDYVILHELCHLKVHNHGKGFYRL 223
Cdd:cd07344    1 AKELLPERVEKYAERLG--VKPPKIRIRDMKTRWGSCSSKGNINLNWRLIKAPPEVIDYVVVHELAHLKHMNHSPRFWAL 78

                         90
                 ....*....|....*.
gi 493494014 224 LDAHLPGWRGIKQRLD 239
Cdd:cd07344   79 VERYMPDYKERRKWLK 94
 
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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