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Conserved domains on  [gi|651901302|ref|WP_026656344|]
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MULTISPECIES: PEGA domain-containing protein [Butyrivibrio]

Protein Classification

peptidase associated/transthyretin-like domain-containing protein( domain architecture ID 229422)

peptidase associated/transthyretin-like domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Peptidase_M14NE-CP-C_like super family cl21470
Peptidase associated domain: C-terminal domain of M14 N/E carboxypeptidase; putative folding, ...
 406-459 2.43e-06

Peptidase associated domain: C-terminal domain of M14 N/E carboxypeptidase; putative folding, regulation, or interaction domain; This domain is found C-terminal to the M14 carboxypeptidase (CP) N/E subfamily containing zinc-binding enzymes that hydrolyze single C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. The N/E subfamily includes enzymatically active members (carboxypeptidase N, E, M, D, and Z), as well as non-active members (carboxypeptidase-like protein 1, -2, aortic CP-like protein, and adipocyte enhancer binding protein-1) which lack the critical active site and substrate-binding residues considered necessary for activity. The active N/E enzymes fulfill a variety of cellular functions, including prohormone processing, regulation of peptide hormone activity, alteration of protein-protein or protein-cell interactions and transcriptional regulation. For M14 CPs, it has been suggested that this domain may assist in folding of the CP domain, regulate enzyme activity, or be involved in interactions with other proteins or with membranes; for carboxypeptidase M, it may interact with the bradykinin 1 receptor at the cell surface. This domain may also be found in other peptidase families.


The actual alignment was detected with superfamily member pfam08308:

Pssm-ID: 473874 [Multi-domain]  Cd Length: 71  Bit Score: 45.37  E-value: 2.43e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 651901302  406 VYVDS-PEGAELFFDGNYIGVVPTSLKKV-SGNHEIILRKNGYNTKSLRVNIDADE 459
Cdd:pfam08308   4 LSITSnPEGATVYIDGNYLGKTPVTVSDLpAGTYSVRLEKEGYEDYEKTVTVTAGE 59
MSCRAMM_ClfA super family cl41352
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 467-601 8.87e-03

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


The actual alignment was detected with superfamily member NF033609:

Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 39.12  E-value: 8.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651901302 467 GEMAKVKEDTETKPKSEESPTAASTEKQAENPSKAASESTTHDLGKKETPSSSEKSDTSAATEKTTATAHYASTASSEED 546
Cdd:NF033609 552 GEIEPIPEDSDSDPGSDSGSDSSNSDSGSDSGSDSTSDSGSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSA 631

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 651901302 547 ESPSKKSTADAANKSSTKEDETTSVNKKDSDNKDGKKAGDNKDKTGKDKNNNSDA 601
Cdd:NF033609 632 SDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 686
 
Name Accession Description Interval E-value
PEGA pfam08308
PEGA domain; This domain is found in both archaea and bacteria and has similarity to S-layer ...
 406-459 2.43e-06

PEGA domain; This domain is found in both archaea and bacteria and has similarity to S-layer (surface layer) proteins. It is named after the characteriztic PEGA sequence motif found in this domain. The secondary structure of this domain is predicted to be beta-strands [Adindla et al. Comparative and Functional Genomics 2004; 5:2-16].


Pssm-ID: 429908 [Multi-domain]  Cd Length: 71  Bit Score: 45.37  E-value: 2.43e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 651901302  406 VYVDS-PEGAELFFDGNYIGVVPTSLKKV-SGNHEIILRKNGYNTKSLRVNIDADE 459
Cdd:pfam08308   4 LSITSnPEGATVYIDGNYLGKTPVTVSDLpAGTYSVRLEKEGYEDYEKTVTVTAGE 59
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 467-601 8.87e-03

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 39.12  E-value: 8.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651901302 467 GEMAKVKEDTETKPKSEESPTAASTEKQAENPSKAASESTTHDLGKKETPSSSEKSDTSAATEKTTATAHYASTASSEED 546
Cdd:NF033609 552 GEIEPIPEDSDSDPGSDSGSDSSNSDSGSDSGSDSTSDSGSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSA 631

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 651901302 547 ESPSKKSTADAANKSSTKEDETTSVNKKDSDNKDGKKAGDNKDKTGKDKNNNSDA 601
Cdd:NF033609 632 SDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 686
 
Name Accession Description Interval E-value
PEGA pfam08308
PEGA domain; This domain is found in both archaea and bacteria and has similarity to S-layer ...
 406-459 2.43e-06

PEGA domain; This domain is found in both archaea and bacteria and has similarity to S-layer (surface layer) proteins. It is named after the characteriztic PEGA sequence motif found in this domain. The secondary structure of this domain is predicted to be beta-strands [Adindla et al. Comparative and Functional Genomics 2004; 5:2-16].


Pssm-ID: 429908 [Multi-domain]  Cd Length: 71  Bit Score: 45.37  E-value: 2.43e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 651901302  406 VYVDS-PEGAELFFDGNYIGVVPTSLKKV-SGNHEIILRKNGYNTKSLRVNIDADE 459
Cdd:pfam08308   4 LSITSnPEGATVYIDGNYLGKTPVTVSDLpAGTYSVRLEKEGYEDYEKTVTVTAGE 59
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 467-601 8.87e-03

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 39.12  E-value: 8.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651901302 467 GEMAKVKEDTETKPKSEESPTAASTEKQAENPSKAASESTTHDLGKKETPSSSEKSDTSAATEKTTATAHYASTASSEED 546
Cdd:NF033609 552 GEIEPIPEDSDSDPGSDSGSDSSNSDSGSDSGSDSTSDSGSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSA 631

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 651901302 547 ESPSKKSTADAANKSSTKEDETTSVNKKDSDNKDGKKAGDNKDKTGKDKNNNSDA 601
Cdd:NF033609 632 SDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 686
 
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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