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Conserved domains on  [gi|1710921022|gb|TVQ81194|]
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T9SS C-terminal target domain-containing protein, partial [Flavobacteriales bacterium]

Protein Classification

T9SS type A sorting domain-containing protein( domain architecture ID 10024511)

T9SS type A sorting domain-containing protein may function in protein secretion; the conserved C-terminal domain functions as an outer membrane translocation signal for export of virulence factors to the cell surface

Gene Ontology:  GO:0005576
PubMed:  24007199

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Por_Secre_tail TIGR04183
Por secretion system C-terminal sorting domain; Species that include Porphyromonas gingivalis, ...
 497-572 9.77e-11

Por secretion system C-terminal sorting domain; Species that include Porphyromonas gingivalis, Fibrobacter succinogenes, Flavobacterium johnsoniae, Cytophaga hutchinsonii, Gramella forsetii, Prevotella intermedia, and Salinibacter ruber average twenty or more copies of a C-terminal domain, represented by this model, associated with sorting to the outer membrane and covalent modification.


:

Pssm-ID: 275036 [Multi-domain]  Cd Length: 72  Bit Score: 57.80  E-value: 9.77e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1710921022 497 LYPNPTSDFLYFKTPGIEDPetpIEISVYNLTGIKVHQdfTQASFLQRIHVENLASGMYVLKVQAKGVIKTQKFLI 572
Cdd:TIGR04183   1 IYPNPAKGTLIIILLSSSGK---VKVEIYDLSGKLVKK--TTLNNSNSIDLSNLSSGVYIVKITTGNGTITKKIIK 71
 
Name Accession Description Interval E-value
Por_Secre_tail TIGR04183
Por secretion system C-terminal sorting domain; Species that include Porphyromonas gingivalis, ...
 497-572 9.77e-11

Por secretion system C-terminal sorting domain; Species that include Porphyromonas gingivalis, Fibrobacter succinogenes, Flavobacterium johnsoniae, Cytophaga hutchinsonii, Gramella forsetii, Prevotella intermedia, and Salinibacter ruber average twenty or more copies of a C-terminal domain, represented by this model, associated with sorting to the outer membrane and covalent modification.


Pssm-ID: 275036 [Multi-domain]  Cd Length: 72  Bit Score: 57.80  E-value: 9.77e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1710921022 497 LYPNPTSDFLYFKTPGIEDPetpIEISVYNLTGIKVHQdfTQASFLQRIHVENLASGMYVLKVQAKGVIKTQKFLI 572
Cdd:TIGR04183   1 IYPNPAKGTLIIILLSSSGK---VKVEIYDLSGKLVKK--TTLNNSNSIDLSNLSSGVYIVKITTGNGTITKKIIK 71
Por_Secre_tail pfam18962
Secretion system C-terminal sorting domain; Species that include Porphyromonas gingivalis, ...
 497-572 5.72e-10

Secretion system C-terminal sorting domain; Species that include Porphyromonas gingivalis, Fibrobacter succinogenes, Flavobacterium johnsoniae, Cytophaga hutchinsonii, Gramella forsetii, Prevotella intermedia, and Salinibacter ruber have on average twenty or more copies of this C-terminal domain, associated with sorting to the outer membrane and covalent modification. This domain targets proteins to type IX secretion systems and is secreted then cleaved off by a C-terminal signal peptidease. Based on similarity to other families it is likely that this domain adopts an immunoglobulin like fold.


Pssm-ID: 436869 [Multi-domain]  Cd Length: 75  Bit Score: 55.69  E-value: 5.72e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1710921022 497 LYPNPTSDFLYFKTPGIEdpETPIEISVYNLTGIKVHQDFTQASFLQ-RIHVENLASGMYVLKVQAKGVIKTQKFLI 572
Cdd:pfam18962   1 IYPNPAKDVLNISLKNSN--SSNLNISIYDILGKLVKSNSKTNGNNTkTIDVSNLSSGIYFVKINSGNGSTTKKLII 75
T9SSA_dep_M36 NF038113
T9SS-dependent M36 family metallopeptidase; Members of this family have an M36 family ...
 498-572 2.94e-04

T9SS-dependent M36 family metallopeptidase; Members of this family have an M36 family metallopeptidase domain, like fungalysin (see PF02128), and a C-terminal T9SS type A sorting domain (see TIGR04131).


Pssm-ID: 468356 [Multi-domain]  Cd Length: 868  Bit Score: 43.87  E-value: 2.94e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1710921022 498 YPNPTSDFLYFKTPGIEDPETpiEISVYNLTGIKVHQDFTQASFLQRIHVENLASGMYVLKVQAKGVIKTQKFLI 572
Cdd:NF038113  795 YPNPAKGEIFISFSNKDSGEV--KVKVYDINGRLVLSDKVELTNTKTINTSGLQSGIYIVKIEGGSKSYTEKLIV 867
 
Name Accession Description Interval E-value
Por_Secre_tail TIGR04183
Por secretion system C-terminal sorting domain; Species that include Porphyromonas gingivalis, ...
 497-572 9.77e-11

Por secretion system C-terminal sorting domain; Species that include Porphyromonas gingivalis, Fibrobacter succinogenes, Flavobacterium johnsoniae, Cytophaga hutchinsonii, Gramella forsetii, Prevotella intermedia, and Salinibacter ruber average twenty or more copies of a C-terminal domain, represented by this model, associated with sorting to the outer membrane and covalent modification.


Pssm-ID: 275036 [Multi-domain]  Cd Length: 72  Bit Score: 57.80  E-value: 9.77e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1710921022 497 LYPNPTSDFLYFKTPGIEDPetpIEISVYNLTGIKVHQdfTQASFLQRIHVENLASGMYVLKVQAKGVIKTQKFLI 572
Cdd:TIGR04183   1 IYPNPAKGTLIIILLSSSGK---VKVEIYDLSGKLVKK--TTLNNSNSIDLSNLSSGVYIVKITTGNGTITKKIIK 71
Por_Secre_tail pfam18962
Secretion system C-terminal sorting domain; Species that include Porphyromonas gingivalis, ...
 497-572 5.72e-10

Secretion system C-terminal sorting domain; Species that include Porphyromonas gingivalis, Fibrobacter succinogenes, Flavobacterium johnsoniae, Cytophaga hutchinsonii, Gramella forsetii, Prevotella intermedia, and Salinibacter ruber have on average twenty or more copies of this C-terminal domain, associated with sorting to the outer membrane and covalent modification. This domain targets proteins to type IX secretion systems and is secreted then cleaved off by a C-terminal signal peptidease. Based on similarity to other families it is likely that this domain adopts an immunoglobulin like fold.


Pssm-ID: 436869 [Multi-domain]  Cd Length: 75  Bit Score: 55.69  E-value: 5.72e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1710921022 497 LYPNPTSDFLYFKTPGIEdpETPIEISVYNLTGIKVHQDFTQASFLQ-RIHVENLASGMYVLKVQAKGVIKTQKFLI 572
Cdd:pfam18962   1 IYPNPAKDVLNISLKNSN--SSNLNISIYDILGKLVKSNSKTNGNNTkTIDVSNLSSGIYFVKINSGNGSTTKKLII 75
T9SSA_dep_M36 NF038113
T9SS-dependent M36 family metallopeptidase; Members of this family have an M36 family ...
 498-572 2.94e-04

T9SS-dependent M36 family metallopeptidase; Members of this family have an M36 family metallopeptidase domain, like fungalysin (see PF02128), and a C-terminal T9SS type A sorting domain (see TIGR04131).


Pssm-ID: 468356 [Multi-domain]  Cd Length: 868  Bit Score: 43.87  E-value: 2.94e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1710921022 498 YPNPTSDFLYFKTPGIEDPETpiEISVYNLTGIKVHQDFTQASFLQRIHVENLASGMYVLKVQAKGVIKTQKFLI 572
Cdd:NF038113  795 YPNPAKGEIFISFSNKDSGEV--KVKVYDINGRLVLSDKVELTNTKTINTSGLQSGIYIVKIEGGSKSYTEKLIV 867
 
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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