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Conserved domains on  [gi|504292611|ref|WP_014479713|]
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MULTISPECIES: CAP domain-containing protein [Bacillus]

Protein Classification

CAP domain-containing protein( domain architecture ID 12168137)

CAP (CSP/antigen 5/PR1) domain-containing protein similar to Bacillus subtilis membrane protein YlbC and Staphylococcus aureus cysteine-rich secretory protein SAV1118

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CAP_assoc_N pfam14504
CAP-associated N-terminal; The function of this domain is unknown, but it is found towards the ...
 61-200 1.21e-65

CAP-associated N-terminal; The function of this domain is unknown, but it is found towards the N-terminus of bacterial proteins carrying the CAP domain, pfam00188. All members that do not otherwise carry an additional Cu_amine_oxidN1, pfam07833, domain are likely to be extracellular as they start with a signal-peptide. Most other non-bacterial proteins with the CAP domain are allergenic.


:

Pssm-ID: 433999  Cd Length: 140  Bit Score: 203.58  E-value: 1.21e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504292611   61 MGKPADEVTKKLGEPERIDPSAYDYDWWVYNQGKDQYIQIGVLNNKVVTLFASGNDINAKPFKIGESTGEVFKTTQVAPF 140
Cdd:pfam14504   1 IGKSVEEVEEKLGEPDRKDPSAYGYEWWVYNQDYNQYIQVGVDDGKVVTLYTNGDDVNVAPFKIGTSKEEVFKKLGIPLN 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 504292611  141 VNVEYKGNSYRFEFSEEDINTRPTVKVGKMYVQLYMDKFEGKLSSIRAFDAQTFVKQRPY 200
Cdd:pfam14504  81 VSFEIKKGSYRFELSEEDLNERPLVAVDGTYAQLFFDHFTNKVTSVRYLDKETLLKLRPY 140
YkwD COG2340
Spore germination protein YkwD and related proteins with CAP (CSP/antigen 5/PR1) domain [Cell ...
 223-345 9.83e-49

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: 160.55  E-value: 9.83e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504292611 223 QTTSEKQILDLTNVIRVKHGLAKLEWDQPTAEVAFGHSEDMKENNYFSHVSKKYGSLKDRLEEGHVDFQQAGENIAYNYV 302
Cdd:COG2340   17 LSALEQEVLELVNAYRAAAGLPPLTWDPRLTAAARAHAQDMAENGYFSHTGPDGSSPFDRLKAAGYSYRAAGENIAAGYS 96

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 504292611 303 DGPAAVEGWLNSEGHRKALLNSDYTHLGVGV-----DRKYYTQNFIKR 345
Cdd:COG2340   97 TAEEAVDGWMNSPGHRANILNPDFTEIGVGVayggdGGVYWTQVFGRP 144
 
Name Accession Description Interval E-value
CAP_assoc_N pfam14504
CAP-associated N-terminal; The function of this domain is unknown, but it is found towards the ...
 61-200 1.21e-65

CAP-associated N-terminal; The function of this domain is unknown, but it is found towards the N-terminus of bacterial proteins carrying the CAP domain, pfam00188. All members that do not otherwise carry an additional Cu_amine_oxidN1, pfam07833, domain are likely to be extracellular as they start with a signal-peptide. Most other non-bacterial proteins with the CAP domain are allergenic.


Pssm-ID: 433999  Cd Length: 140  Bit Score: 203.58  E-value: 1.21e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504292611   61 MGKPADEVTKKLGEPERIDPSAYDYDWWVYNQGKDQYIQIGVLNNKVVTLFASGNDINAKPFKIGESTGEVFKTTQVAPF 140
Cdd:pfam14504   1 IGKSVEEVEEKLGEPDRKDPSAYGYEWWVYNQDYNQYIQVGVDDGKVVTLYTNGDDVNVAPFKIGTSKEEVFKKLGIPLN 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 504292611  141 VNVEYKGNSYRFEFSEEDINTRPTVKVGKMYVQLYMDKFEGKLSSIRAFDAQTFVKQRPY 200
Cdd:pfam14504  81 VSFEIKKGSYRFELSEEDLNERPLVAVDGTYAQLFFDHFTNKVTSVRYLDKETLLKLRPY 140
YkwD COG2340
Spore germination protein YkwD and related proteins with CAP (CSP/antigen 5/PR1) domain [Cell ...
 223-345 9.83e-49

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: 160.55  E-value: 9.83e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504292611 223 QTTSEKQILDLTNVIRVKHGLAKLEWDQPTAEVAFGHSEDMKENNYFSHVSKKYGSLKDRLEEGHVDFQQAGENIAYNYV 302
Cdd:COG2340   17 LSALEQEVLELVNAYRAAAGLPPLTWDPRLTAAARAHAQDMAENGYFSHTGPDGSSPFDRLKAAGYSYRAAGENIAAGYS 96

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 504292611 303 DGPAAVEGWLNSEGHRKALLNSDYTHLGVGV-----DRKYYTQNFIKR 345
Cdd:COG2340   97 TAEEAVDGWMNSPGHRANILNPDFTEIGVGVayggdGGVYWTQVFGRP 144
CAP_bacterial cd05379
Bacterial CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 ...
 227-343 3.36e-40

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: 137.51  E-value: 3.36e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504292611 227 EKQILDLTNVIRVKHGLAKLEWDQPTAEVAFGHSEDMKENNYFSHVSKKYGSlkDRLEEGHVDFQQAGENIAYNYVDGPA 306
Cdd:cd05379    1 EQEVLELINEYRAKAGLPPLSWDPRLEKAAQDHAEDMAANGYFSHTGPDGSS--DRAARAGYWYRGAGENIAYGQGSAEE 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 504292611 307 AVEGWLNSEGHRKALLNSDYTHLGVGV-----DRKYYTQNFI 343
Cdd:cd05379   79 AVNQWINSPGHRANILDPDFTEIGVGVaynssGGTYWTQVFG 120
spore_YkwD TIGR02909
uncharacterized protein, YkwD family; Members of this protein family represent a subset of ...
 227-344 2.82e-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: 2.82e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504292611  227 EKQILDLTNVIRVKHGLAKLEWDQPTAEVAFGHSEDMKENNYFSHVSKKYGSLKDRLEEGHVDFQQAGENIAYNYVDGPA 306
Cdd:TIGR02909   5 EKRVVELVNAERAKNGLKPLKADPELSKVARLKSEDMRDKNYFSHTSPTYGSPFDMMKKFGISYRMAGENIAYGNSTVEA 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 504292611  307 AVEGWLNSEGHRKALLNSDYTHLGVGVDR-----KYYTQNFIK 344
Cdd:TIGR02909  85 VHNAWMNSPGHRANILNPNYTEIGVGYVEggsggIYWTQMFIG 127
CAP pfam00188
Cysteine-rich secretory protein family; This is a large family of cysteine-rich secretory ...
 231-342 1.04e-16

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: 75.32  E-value: 1.04e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504292611  231 LDLTNVIRVKHGLAKLEWDQPTAEVAFGHSEDMKENNYFSHVSKKYGSLKDRLEEGHVDFQQAGENIAYnyvdgpAAVEG 310
Cdd:pfam00188   1 LDLHNEYRAAAGLPPLSWDNELAAAAQDHAKYCADNGSHNHRSPYGGNIYARVVAAGYALGDAGPDSAE------DAVDG 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 504292611  311 WLNSE-----GHRKALLNSDYTHLGVGV------DRKYYTQNF 342
Cdd:pfam00188  75 WYDSPgtyncGHRTNLLWPKSTKVGCAVakcgdgGTYYFVCNY 117
 
Name Accession Description Interval E-value
CAP_assoc_N pfam14504
CAP-associated N-terminal; The function of this domain is unknown, but it is found towards the ...
 61-200 1.21e-65

CAP-associated N-terminal; The function of this domain is unknown, but it is found towards the N-terminus of bacterial proteins carrying the CAP domain, pfam00188. All members that do not otherwise carry an additional Cu_amine_oxidN1, pfam07833, domain are likely to be extracellular as they start with a signal-peptide. Most other non-bacterial proteins with the CAP domain are allergenic.


Pssm-ID: 433999  Cd Length: 140  Bit Score: 203.58  E-value: 1.21e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504292611   61 MGKPADEVTKKLGEPERIDPSAYDYDWWVYNQGKDQYIQIGVLNNKVVTLFASGNDINAKPFKIGESTGEVFKTTQVAPF 140
Cdd:pfam14504   1 IGKSVEEVEEKLGEPDRKDPSAYGYEWWVYNQDYNQYIQVGVDDGKVVTLYTNGDDVNVAPFKIGTSKEEVFKKLGIPLN 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 504292611  141 VNVEYKGNSYRFEFSEEDINTRPTVKVGKMYVQLYMDKFEGKLSSIRAFDAQTFVKQRPY 200
Cdd:pfam14504  81 VSFEIKKGSYRFELSEEDLNERPLVAVDGTYAQLFFDHFTNKVTSVRYLDKETLLKLRPY 140
YkwD COG2340
Spore germination protein YkwD and related proteins with CAP (CSP/antigen 5/PR1) domain [Cell ...
 223-345 9.83e-49

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: 160.55  E-value: 9.83e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504292611 223 QTTSEKQILDLTNVIRVKHGLAKLEWDQPTAEVAFGHSEDMKENNYFSHVSKKYGSLKDRLEEGHVDFQQAGENIAYNYV 302
Cdd:COG2340   17 LSALEQEVLELVNAYRAAAGLPPLTWDPRLTAAARAHAQDMAENGYFSHTGPDGSSPFDRLKAAGYSYRAAGENIAAGYS 96

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 504292611 303 DGPAAVEGWLNSEGHRKALLNSDYTHLGVGV-----DRKYYTQNFIKR 345
Cdd:COG2340   97 TAEEAVDGWMNSPGHRANILNPDFTEIGVGVayggdGGVYWTQVFGRP 144
CAP_bacterial cd05379
Bacterial CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 ...
 227-343 3.36e-40

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: 137.51  E-value: 3.36e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504292611 227 EKQILDLTNVIRVKHGLAKLEWDQPTAEVAFGHSEDMKENNYFSHVSKKYGSlkDRLEEGHVDFQQAGENIAYNYVDGPA 306
Cdd:cd05379    1 EQEVLELINEYRAKAGLPPLSWDPRLEKAAQDHAEDMAANGYFSHTGPDGSS--DRAARAGYWYRGAGENIAYGQGSAEE 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 504292611 307 AVEGWLNSEGHRKALLNSDYTHLGVGV-----DRKYYTQNFI 343
Cdd:cd05379   79 AVNQWINSPGHRANILDPDFTEIGVGVaynssGGTYWTQVFG 120
spore_YkwD TIGR02909
uncharacterized protein, YkwD family; Members of this protein family represent a subset of ...
 227-344 2.82e-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: 2.82e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504292611  227 EKQILDLTNVIRVKHGLAKLEWDQPTAEVAFGHSEDMKENNYFSHVSKKYGSLKDRLEEGHVDFQQAGENIAYNYVDGPA 306
Cdd:TIGR02909   5 EKRVVELVNAERAKNGLKPLKADPELSKVARLKSEDMRDKNYFSHTSPTYGSPFDMMKKFGISYRMAGENIAYGNSTVEA 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 504292611  307 AVEGWLNSEGHRKALLNSDYTHLGVGVDR-----KYYTQNFIK 344
Cdd:TIGR02909  85 VHNAWMNSPGHRANILNPNYTEIGVGYVEggsggIYWTQMFIG 127
CAP pfam00188
Cysteine-rich secretory protein family; This is a large family of cysteine-rich secretory ...
 231-342 1.04e-16

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: 75.32  E-value: 1.04e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504292611  231 LDLTNVIRVKHGLAKLEWDQPTAEVAFGHSEDMKENNYFSHVSKKYGSLKDRLEEGHVDFQQAGENIAYnyvdgpAAVEG 310
Cdd:pfam00188   1 LDLHNEYRAAAGLPPLSWDNELAAAAQDHAKYCADNGSHNHRSPYGGNIYARVVAAGYALGDAGPDSAE------DAVDG 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 504292611  311 WLNSE-----GHRKALLNSDYTHLGVGV------DRKYYTQNF 342
Cdd:pfam00188  75 WYDSPgtyncGHRTNLLWPKSTKVGCAVakcgdgGTYYFVCNY 117
CAP cd00168
CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain ...
 229-343 1.57e-15

CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain family; The CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain, also called SCP (sperm-coating glycoprotein), is found in eukaryotes and prokaryotes. This family includes plant pathogenesis-related protein 1 (PR-1), which accumulates after infections with pathogens, and may act as an anti-fungal agent or be involved in cell wall loosening. This family also includes CRISPs (cysteine-rich secretory proteins), which combine the CAP/SCP domain with a C-terminal cysteine rich domain, and allergen 5 from vespid venom. Roles for CRISP, in response to pathogens, fertilization, and sperm maturation have been proposed. One member, Tex31 from the venom duct of Conus textile, has been shown to possess proteolytic activity sensitive to serine protease inhibitors. The human GAPR-1 protein has been reported to dimerize, and such a dimer may form an active site containing a catalytic triad. CAP/SCP has also been proposed to be a Ca++ chelating serine protease. The Ca++-chelating function would fit with various signaling processes that members of this family, such as the CRISPs, are involved in, and is supported by sequence and structural evidence of a conserved pocket containing two histidines and a glutamate. It also may explain how helothermine, a toxic peptide secreted by the beaded lizard, blocks Ca++ transporting ryanodine receptors. Little is known about the biological roles of the bacterial and archaeal CAP/SCP domains.


Pssm-ID: 349397  Cd Length: 128  Bit Score: 72.27  E-value: 1.57e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504292611 229 QILDLTNVIRVKH-----GLAKLEWDQPTAEVAFGHSEDMkennYFSHVSKKYGslkdrleeghvdfQQAGENIAYNY-- 301
Cdd:cd00168    3 EILDLHNSYRSSVsppasNMPLMAWDQELADVAIGYAKDC----IFSHSSPTSR-------------QLAGENIAASSyd 65

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504292611 302 VDGPAAVEGWLNS----------------EGHRKALLNSDYTHLGVGV-----DRKYYTQNFI 343
Cdd:cd00168   66 MDGVAALQAWHNEiknynfgtaqpgfnsgTGHYTQMVWEKTTKLGCGVadcsdNSKFVVCNYI 128
CAP_PRY1-like cd05384
CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain ...
 227-340 1.14e-05

CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain of pathogen-related yeast 1 (PRY1) protein and similar fungal proteins; PRY1, also called pathogenesis-related protein 1, is a yeast protein that is up-regulated in core ESCRT mutants. It is a secreted protein required for efficient export of lipids such as acetylated sterols, and acts in detoxification of hydrophobic compounds. This PRY1-like group also contains fruiting body proteins SC7/14 from Schizophyllum commune. 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.


Pssm-ID: 349403  Cd Length: 129  Bit Score: 44.25  E-value: 1.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504292611 227 EKQILDLTNVIRVKHGLAKLEWDQPTAEVAFGHSEDMKENNYFSHVSKKYGslkdrleeghvdfqqagENIAYNYVDGPA 306
Cdd:cd05384    3 ASSILDAHNKKRALHGTQPLTWNDTLAEYAQDYADSYDCSGNLVHSGGPYG-----------------ENLALGYSSGAA 65

                         90       100       110
                 ....*....|....*....|....*....|....
gi 504292611 307 AVEGWLNsEGHrkallNSDYTHLGVGVDRKYYTQ 340
Cdd:cd05384   66 AVDAWYD-EIS-----DYDYSNPGFSESTGHFTQ 93
CAP_PR-1 cd05381
CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain ...
 228-313 7.56e-04

CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain of pathogenesis-related protein 1 (PR-1) family proteins; Members of pathogenesis-related protein 1 (PR-1) family are among the most abundantly produced proteins in plants on pathogen attack. They are considered hallmarks of hypersensitive response/defense pathways and may act as anti-fungal agents or be involved in cell wall loosening.


Pssm-ID: 349400  Cd Length: 136  Bit Score: 39.15  E-value: 7.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504292611 228 KQILDLTNVIRVKHGLAKLEWDQPTAEVAFGHSEDMKENNYFSHVSKKYgslkdrleeghvdfqqaGENIAYNYVD---G 304
Cdd:cd05381    2 QDFLDAHNQARAAVGVPPLVWDDTLAAYAQKYANQRRGDCSLVHSNGPY-----------------GENLFWGSGDnwsP 64


                 ....*....
gi 504292611 305 PAAVEGWLN 313
Cdd:cd05381   65 ADAVKSWVD 73
 
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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