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Conserved domains on  [gi|530420415|ref|XP_005261818|]
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protein GUCD1 isoform X1 [Homo sapiens]

Protein Classification

cysteine peptidase family C39 domain-containing protein( domain architecture ID 2867)

cysteine peptidase family C39 domain-containing protein, similar to Niallia circulans butirosin biosynthesis protein H

PubMed:  11517925

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Guanylate_cyc_2 super family cl48071
Guanylylate cyclase; Members of this family of proteins catalyze the conversion of guanosine ...
 78-185 8.63e-67

Guanylylate cyclase; Members of this family of proteins catalyze the conversion of guanosine triphosphate (GTP) to 3',5'-cyclic guanosine monophosphate (cGMP) and pyrophosphate.


The actual alignment was detected with superfamily member pfam09778:

Pssm-ID: 462894  Cd Length: 212  Bit Score: 203.64  E-value: 8.63e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420415   78 VPVIQQLYHWDCGLACSRMVLRYLGQLD--DSEFERALQKLQLTRSIWTIDLAYLMHHFGVRHRFCTQTLGVDKGYKNQS 155
Cdd:pfam09778   1 VPHIQQRYNWDCGLACVLMVLRTLGQRScfLKNFEEICKEEGFTTSIWTIDLAYLLKRFGVRHRFYTQTLGVNPNYKNQS 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 530420415  156 FYRKHFDTEETRVNQLFAQAKACKVLVEKC 185
Cdd:pfam09778  81 FYKKTFDKDEKRVNKLFAKAKACGIDVEKR 110
 
Name Accession Description Interval E-value
Guanylate_cyc_2 pfam09778
Guanylylate cyclase; Members of this family of proteins catalyze the conversion of guanosine ...
 78-185 8.63e-67

Guanylylate cyclase; Members of this family of proteins catalyze the conversion of guanosine triphosphate (GTP) to 3',5'-cyclic guanosine monophosphate (cGMP) and pyrophosphate.


Pssm-ID: 462894  Cd Length: 212  Bit Score: 203.64  E-value: 8.63e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420415   78 VPVIQQLYHWDCGLACSRMVLRYLGQLD--DSEFERALQKLQLTRSIWTIDLAYLMHHFGVRHRFCTQTLGVDKGYKNQS 155
Cdd:pfam09778   1 VPHIQQRYNWDCGLACVLMVLRTLGQRScfLKNFEEICKEEGFTTSIWTIDLAYLLKRFGVRHRFYTQTLGVNPNYKNQS 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 530420415  156 FYRKHFDTEETRVNQLFAQAKACKVLVEKC 185
Cdd:pfam09778  81 FYKKTFDKDEKRVNKLFAKAKACGIDVEKR 110
Peptidase_C39F cd02425
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ...
 78-102 1.11e-03

A sub-family of peptidase family C39. Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The cysteine peptidases in family C39 cleave the "double-glycine" leader peptides from the precursors of various bacteriocins (mostly non-lantibiotic). The cleavage is mediated by the transporter as part of the secretion process. Bacteriocins are antibiotic proteins secreted by some species of bacteria that inhibit the growth of other bacterial species. The bacteriocin is synthesized as a precursor with an N-terminal leader peptide, and processing involves removal of the leader peptide by cleavage at a Gly-Gly bond, followed by translocation of the mature bacteriocin across the cytoplasmic membrane. Most endopeptidases of family C39 are N-terminal domains in larger proteins (ABC transporters) that serve both functions. The proposed protease active site is conserved in this sub-family.


Pssm-ID: 239105 [Multi-domain]  Cd Length: 126  Bit Score: 37.63  E-value: 1.11e-03
                         10        20
                 ....*....|....*....|....*
gi 530420415  78 VPVIQQLYHWDCGLACSRMVLRYLG 102
Cdd:cd02425    1 VKPILQNNQTECGLACYAMILNYFG 25
 
Name Accession Description Interval E-value
Guanylate_cyc_2 pfam09778
Guanylylate cyclase; Members of this family of proteins catalyze the conversion of guanosine ...
 78-185 8.63e-67

Guanylylate cyclase; Members of this family of proteins catalyze the conversion of guanosine triphosphate (GTP) to 3',5'-cyclic guanosine monophosphate (cGMP) and pyrophosphate.


Pssm-ID: 462894  Cd Length: 212  Bit Score: 203.64  E-value: 8.63e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420415   78 VPVIQQLYHWDCGLACSRMVLRYLGQLD--DSEFERALQKLQLTRSIWTIDLAYLMHHFGVRHRFCTQTLGVDKGYKNQS 155
Cdd:pfam09778   1 VPHIQQRYNWDCGLACVLMVLRTLGQRScfLKNFEEICKEEGFTTSIWTIDLAYLLKRFGVRHRFYTQTLGVNPNYKNQS 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 530420415  156 FYRKHFDTEETRVNQLFAQAKACKVLVEKC 185
Cdd:pfam09778  81 FYKKTFDKDEKRVNKLFAKAKACGIDVEKR 110
Peptidase_C39F cd02425
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ...
 78-102 1.11e-03

A sub-family of peptidase family C39. Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The cysteine peptidases in family C39 cleave the "double-glycine" leader peptides from the precursors of various bacteriocins (mostly non-lantibiotic). The cleavage is mediated by the transporter as part of the secretion process. Bacteriocins are antibiotic proteins secreted by some species of bacteria that inhibit the growth of other bacterial species. The bacteriocin is synthesized as a precursor with an N-terminal leader peptide, and processing involves removal of the leader peptide by cleavage at a Gly-Gly bond, followed by translocation of the mature bacteriocin across the cytoplasmic membrane. Most endopeptidases of family C39 are N-terminal domains in larger proteins (ABC transporters) that serve both functions. The proposed protease active site is conserved in this sub-family.


Pssm-ID: 239105 [Multi-domain]  Cd Length: 126  Bit Score: 37.63  E-value: 1.11e-03
                         10        20
                 ....*....|....*....|....*
gi 530420415  78 VPVIQQLYHWDCGLACSRMVLRYLG 102
Cdd:cd02425    1 VKPILQNNQTECGLACYAMILNYFG 25
Peptidase_C39 pfam03412
Peptidase C39 family; Lantibiotic and non-lantibiotic bacteriocins are synthesized as ...
 78-102 3.96e-03

Peptidase C39 family; Lantibiotic and non-lantibiotic bacteriocins are synthesized as precursor peptides containing N-terminal extensions (leader peptides) which are cleaved off during maturation. Most non-lantibiotics and also some lantibiotics have leader peptides of the so-called double-glycine type. These leader peptides share consensus sequences and also a common processing site with two conserved glycine residues in positions -1 and -2. The double- glycine-type leader peptides are unrelated to the N-terminal signal sequences which direct proteins across the cytoplasmic membrane via the sec pathway. Their processing sites are also different from typical signal peptidase cleavage sites, suggesting that a different processing enzyme is involved. Peptide bacteriocins are exported across the cytoplasmic membrane by a dedicated ATP-binding cassette (ABC) transporter. The ABC transporter is the maturation protease and its proteolytic domain resides in the N-terminal part of the protein. This peptidase domain is found in a wide range of ABC transporters, however the presumed catalytic cysteine and histidine are not conserved in all members of this family.


Pssm-ID: 367483 [Multi-domain]  Cd Length: 133  Bit Score: 36.05  E-value: 3.96e-03
                          10        20
                  ....*....|....*....|....*
gi 530420415   78 VPVIQQLYHWDCGLACSRMVLRYLG 102
Cdd:pfam03412   2 YKIVLQVDENDCGLACLAMILKYYG 26
 
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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