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Conserved domains on  [gi|818736209|gb|KKT79162|]
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SCP-like protein extracellular [Candidatus Giovannonibacteria bacterium GW2011_GWC2_44_8]

Protein Classification

CAP domain-containing protein( domain architecture ID 11457140)

CAP (CSP/antigen 5/PR1) domain-containing protein

CATH:  3.40.33.10
PubMed:  18824526
SCOP:  4001882

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YkwD COG2340
Spore germination protein YkwD and related proteins with CAP (CSP/antigen 5/PR1) domain [Cell ...
 66-189 4.14e-43

Spore germination protein YkwD and related proteins with CAP (CSP/antigen 5/PR1) domain [Cell cycle control, cell division, chromosome partitioning, General function prediction only];


:

Pssm-ID: 441910  Cd Length: 144  Bit Score: 145.14  E-value: 4.14e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736209  66 LVDETNTRRAEQDLAPLKTNHLLENAAKMKADDMATKGYFSHATPDGKTPWYFLDKAGYVFSAAGENLAVNFFDSKDVAE 145
Cdd:COG2340   24 VLELVNAYRAAAGLPPLTWDPRLTAAARAHAQDMAENGYFSHTGPDGSSPFDRLKAAGYSYRAAGENIAAGYSTAEEAVD 103

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 818736209 146 AWMNSAGHRANMLNSNYTEIGIATArgiYDGREAIFVVQFFGTP 189
Cdd:COG2340  104 GWMNSPGHRANILNPDFTEIGVGVA---YGGDGGVYWTQVFGRP 144
 
Name Accession Description Interval E-value
YkwD COG2340
Spore germination protein YkwD and related proteins with CAP (CSP/antigen 5/PR1) domain [Cell ...
 66-189 4.14e-43

Spore germination protein YkwD and related proteins with CAP (CSP/antigen 5/PR1) domain [Cell cycle control, cell division, chromosome partitioning, General function prediction only];


Pssm-ID: 441910  Cd Length: 144  Bit Score: 145.14  E-value: 4.14e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736209  66 LVDETNTRRAEQDLAPLKTNHLLENAAKMKADDMATKGYFSHATPDGKTPWYFLDKAGYVFSAAGENLAVNFFDSKDVAE 145
Cdd:COG2340   24 VLELVNAYRAAAGLPPLTWDPRLTAAARAHAQDMAENGYFSHTGPDGSSPFDRLKAAGYSYRAAGENIAAGYSTAEEAVD 103

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 818736209 146 AWMNSAGHRANMLNSNYTEIGIATArgiYDGREAIFVVQFFGTP 189
Cdd:COG2340  104 GWMNSPGHRANILNPDFTEIGVGVA---YGGDGGVYWTQVFGRP 144
spore_YkwD TIGR02909
uncharacterized protein, YkwD family; Members of this protein family represent a subset of ...
 66-186 1.41e-35

uncharacterized protein, YkwD family; Members of this protein family represent a subset of those belonging to pfam00188 (SCP-like extracellular protein). Based on currently cuttoffs for this model, all member proteins are found in Bacteria capable of endospore formation. Members include a named but uncharacterized protein, YkwD of Bacillus subtilis. Only the C-terminal region is well-conserved and is included in the seed alignment for this model. Three members of this family have an N-terminal domain homologous to the spore coat assembly protein SafA.


Pssm-ID: 131955  Cd Length: 127  Bit Score: 124.85  E-value: 1.41e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736209   66 LVDETNTRRAEQDLAPLKTNHLLENAAKMKADDMATKGYFSHATPDGKTPWYFLDKAGYVFSAAGENLAVNFFDSKDVAE 145
Cdd:TIGR02909   8 VVELVNAERAKNGLKPLKADPELSKVARLKSEDMRDKNYFSHTSPTYGSPFDMMKKFGISYRMAGENIAYGNSTVEAVHN 87

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 818736209  146 AWMNSAGHRANMLNSNYTEIGIATARGiydGREAIFVVQFF 186
Cdd:TIGR02909  88 AWMNSPGHRANILNPNYTEIGVGYVEG---GSGGIYWTQMF 125
CAP_bacterial cd05379
Bacterial CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 ...
 66-187 4.11e-34

Bacterial CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain proteins; Little is known about bacterial and archaeal members of the CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain family. The wider family of CAP domain containing proteins includes plant pathogenesis-related protein 1 (PR-1), cysteine-rich secretory proteins (CRISPs), and allergen 5 from vespid venom, among others. Studies of eukaryotic proteins show that CAP domains have several functions, including the binding of cholesterol, lipids and heparan sulfate. This group includes Borrelia burgdorferi outer surface protein BB0689, which does not bind to cholesterol, lipids, or heparan sulfate, and whose function is unknown.


Pssm-ID: 349398  Cd Length: 120  Bit Score: 120.95  E-value: 4.11e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736209  66 LVDETNTRRAEQDLAPLKTNHLLENAAKMKADDMATKGYFSHATPDGKTPWYflDKAGYVFSAAGENLAVNFFDSKDVAE 145
Cdd:cd05379    4 VLELINEYRAKAGLPPLSWDPRLEKAAQDHAEDMAANGYFSHTGPDGSSDRA--ARAGYWYRGAGENIAYGQGSAEEAVN 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 818736209 146 AWMNSAGHRANMLNSNYTEIGIATArgiYDGREAIFVVQFFG 187
Cdd:cd05379   82 QWINSPGHRANILDPDFTEIGVGVA---YNSSGGTYWTQVFG 120
CAP pfam00188
Cysteine-rich secretory protein family; This is a large family of cysteine-rich secretory ...
 67-185 8.17e-23

Cysteine-rich secretory protein family; This is a large family of cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins (CAP) that are found in a wide range of organizms, including prokaryotes and non-vertebrate eukaryotes, The nine subfamilies of the mammalian CAP 'super'family include: the human glioma pathogenesis-related 1 (GLIPR1), Golgi associated pathogenesis related-1 (GAPR1) proteins, peptidase inhibitor 15 (PI15), peptidase inhibitor 16 (PI16), cysteine-rich secretory proteins (CRISPs), CRISP LCCL domain containing 1 (CRISPLD1), CRISP LCCL domain containing 2 (CRISPLD2), mannose receptor like and the R3H domain containing like proteins. Members are most often secreted and have an extracellular endocrine or paracrine function and are involved in processes including the regulation of extracellular matrix and branching morphogenesis, potentially as either proteases or protease inhibitors; in ion channel regulation in fertility; as tumour suppressor or pro-oncogenic genes in tissues including the prostate; and in cell-cell adhesion during fertilization. The overall protein structural conservation within the CAP 'super'family results in fundamentally similar functions for the CAP domain in all members, yet the diversity outside of this core region dramatically alters the target specificity and, thus, the biological consequences. The Ca++-chelating function would fit with the various signalling processes (e.g. the CRISP proteins) that members of this family are involved in, and also the sequence and structural evidence of a conserved pocket containing two histidines and a glutamate. It also may explain how Swiss:Q91055 blocks the Ca++ transporting ryanodine receptors.


Pssm-ID: 395136  Cd Length: 117  Bit Score: 91.11  E-value: 8.17e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736209   67 VDETNTRRAEQDLAPLKTNHLLENAAKMKADDMATKGYFSHATPDGKTPWYFLDKAGYVFSAAGENLAvnffdsKDVAEA 146
Cdd:pfam00188   1 LDLHNEYRAAAGLPPLSWDNELAAAAQDHAKYCADNGSHNHRSPYGGNIYARVVAAGYALGDAGPDSA------EDAVDG 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 818736209  147 WMNSA-----GHRANMLNSNYTEIGIATARGiYDGREAIFVVQF 185
Cdd:pfam00188  75 WYDSPgtyncGHRTNLLWPKSTKVGCAVAKC-GDGGTYYFVCNY 117
 
Name Accession Description Interval E-value
YkwD COG2340
Spore germination protein YkwD and related proteins with CAP (CSP/antigen 5/PR1) domain [Cell ...
 66-189 4.14e-43

Spore germination protein YkwD and related proteins with CAP (CSP/antigen 5/PR1) domain [Cell cycle control, cell division, chromosome partitioning, General function prediction only];


Pssm-ID: 441910  Cd Length: 144  Bit Score: 145.14  E-value: 4.14e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736209  66 LVDETNTRRAEQDLAPLKTNHLLENAAKMKADDMATKGYFSHATPDGKTPWYFLDKAGYVFSAAGENLAVNFFDSKDVAE 145
Cdd:COG2340   24 VLELVNAYRAAAGLPPLTWDPRLTAAARAHAQDMAENGYFSHTGPDGSSPFDRLKAAGYSYRAAGENIAAGYSTAEEAVD 103

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 818736209 146 AWMNSAGHRANMLNSNYTEIGIATArgiYDGREAIFVVQFFGTP 189
Cdd:COG2340  104 GWMNSPGHRANILNPDFTEIGVGVA---YGGDGGVYWTQVFGRP 144
spore_YkwD TIGR02909
uncharacterized protein, YkwD family; Members of this protein family represent a subset of ...
 66-186 1.41e-35

uncharacterized protein, YkwD family; Members of this protein family represent a subset of those belonging to pfam00188 (SCP-like extracellular protein). Based on currently cuttoffs for this model, all member proteins are found in Bacteria capable of endospore formation. Members include a named but uncharacterized protein, YkwD of Bacillus subtilis. Only the C-terminal region is well-conserved and is included in the seed alignment for this model. Three members of this family have an N-terminal domain homologous to the spore coat assembly protein SafA.


Pssm-ID: 131955  Cd Length: 127  Bit Score: 124.85  E-value: 1.41e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736209   66 LVDETNTRRAEQDLAPLKTNHLLENAAKMKADDMATKGYFSHATPDGKTPWYFLDKAGYVFSAAGENLAVNFFDSKDVAE 145
Cdd:TIGR02909   8 VVELVNAERAKNGLKPLKADPELSKVARLKSEDMRDKNYFSHTSPTYGSPFDMMKKFGISYRMAGENIAYGNSTVEAVHN 87

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 818736209  146 AWMNSAGHRANMLNSNYTEIGIATARGiydGREAIFVVQFF 186
Cdd:TIGR02909  88 AWMNSPGHRANILNPNYTEIGVGYVEG---GSGGIYWTQMF 125
CAP_bacterial cd05379
Bacterial CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 ...
 66-187 4.11e-34

Bacterial CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain proteins; Little is known about bacterial and archaeal members of the CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain family. The wider family of CAP domain containing proteins includes plant pathogenesis-related protein 1 (PR-1), cysteine-rich secretory proteins (CRISPs), and allergen 5 from vespid venom, among others. Studies of eukaryotic proteins show that CAP domains have several functions, including the binding of cholesterol, lipids and heparan sulfate. This group includes Borrelia burgdorferi outer surface protein BB0689, which does not bind to cholesterol, lipids, or heparan sulfate, and whose function is unknown.


Pssm-ID: 349398  Cd Length: 120  Bit Score: 120.95  E-value: 4.11e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736209  66 LVDETNTRRAEQDLAPLKTNHLLENAAKMKADDMATKGYFSHATPDGKTPWYflDKAGYVFSAAGENLAVNFFDSKDVAE 145
Cdd:cd05379    4 VLELINEYRAKAGLPPLSWDPRLEKAAQDHAEDMAANGYFSHTGPDGSSDRA--ARAGYWYRGAGENIAYGQGSAEEAVN 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 818736209 146 AWMNSAGHRANMLNSNYTEIGIATArgiYDGREAIFVVQFFG 187
Cdd:cd05379   82 QWINSPGHRANILDPDFTEIGVGVA---YNSSGGTYWTQVFG 120
CAP pfam00188
Cysteine-rich secretory protein family; This is a large family of cysteine-rich secretory ...
 67-185 8.17e-23

Cysteine-rich secretory protein family; This is a large family of cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins (CAP) that are found in a wide range of organizms, including prokaryotes and non-vertebrate eukaryotes, The nine subfamilies of the mammalian CAP 'super'family include: the human glioma pathogenesis-related 1 (GLIPR1), Golgi associated pathogenesis related-1 (GAPR1) proteins, peptidase inhibitor 15 (PI15), peptidase inhibitor 16 (PI16), cysteine-rich secretory proteins (CRISPs), CRISP LCCL domain containing 1 (CRISPLD1), CRISP LCCL domain containing 2 (CRISPLD2), mannose receptor like and the R3H domain containing like proteins. Members are most often secreted and have an extracellular endocrine or paracrine function and are involved in processes including the regulation of extracellular matrix and branching morphogenesis, potentially as either proteases or protease inhibitors; in ion channel regulation in fertility; as tumour suppressor or pro-oncogenic genes in tissues including the prostate; and in cell-cell adhesion during fertilization. The overall protein structural conservation within the CAP 'super'family results in fundamentally similar functions for the CAP domain in all members, yet the diversity outside of this core region dramatically alters the target specificity and, thus, the biological consequences. The Ca++-chelating function would fit with the various signalling processes (e.g. the CRISP proteins) that members of this family are involved in, and also the sequence and structural evidence of a conserved pocket containing two histidines and a glutamate. It also may explain how Swiss:Q91055 blocks the Ca++ transporting ryanodine receptors.


Pssm-ID: 395136  Cd Length: 117  Bit Score: 91.11  E-value: 8.17e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818736209   67 VDETNTRRAEQDLAPLKTNHLLENAAKMKADDMATKGYFSHATPDGKTPWYFLDKAGYVFSAAGENLAvnffdsKDVAEA 146
Cdd:pfam00188   1 LDLHNEYRAAAGLPPLSWDNELAAAAQDHAKYCADNGSHNHRSPYGGNIYARVVAAGYALGDAGPDSA------EDAVDG 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 818736209  147 WMNSA-----GHRANMLNSNYTEIGIATARGiYDGREAIFVVQF 185
Cdd:pfam00188  75 WYDSPgtyncGHRTNLLWPKSTKVGCAVAKC-GDGGTYYFVCNY 117
 
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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