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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235992  54 QFLFRHNLVRAARFEPPLIWDRRLQNYAQGWANQRRGDCALRHSvsNGEFnlGENIYWGYGANWSPADAVVAWASEKRFY 133
Cdd:cd05381   3 DFLDAHNQARAAVGVPPLVWDDTLAAYAQKYANQRRGDCSLVHS--NGPY--GENLFWGSGDNWSPADAVKSWVDEKPYY 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15235992 134 HYGSNTCDAGQMCGHYTQIVWKSTRRVGCARVVCDN-GGIFMTCNYDPPGNYIGQKPY 190
Cdd:cd05381  79 DYASNTCVGGKMCGHYTQVVWRNSTRLGCARVVCDNnGGTFVICNYDPPGNYIGERPY 136

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235992  54 QFLFRHNLVRAARFEPPLIWDRRLQNYAQGWANQRRGDCALRHSvsNGEFnlGENIYWGYGANWSPADAVVAWASEKRFY 133
Cdd:cd05381   3 DFLDAHNQARAAVGVPPLVWDDTLAAYAQKYANQRRGDCSLVHS--NGPY--GENLFWGSGDNWSPADAVKSWVDEKPYY 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15235992 134 HYGSNTCDAGQMCGHYTQIVWKSTRRVGCARVVCDN-GGIFMTCNYDPPGNYIGQKPY 190
Cdd:cd05381  79 DYASNTCVGGKMCGHYTQVVWRNSTRLGCARVVCDNnGGTFVICNYDPPGNYIGERPY 136

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235992    56 LFRHNLVRAARFEPPLIWDRRLQNYAQGWANQrrgdCALRHSvSNGEFNLGENIYW---------GYGANWSPADAVVAW 126
Cdd:pfam00188   1 LDLHNEYRAAAGLPPLSWDNELAAAAQDHAKY----CADNGS-HNHRSPYGGNIYArvvaagyalGDAGPDSAEDAVDGW 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 15235992   127 ASEKRFYHygsntcdagqmCGHYTQIVWKSTRRVGCARVVCDNGG-IFMTCNY 178
Cdd:pfam00188  76 YDSPGTYN-----------CGHRTNLLWPKSTKVGCAVAKCGDGGtYYFVCNY 117

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235992  54 QFLFRHNLVRAARFEPPLIWDRRLQNYAQGWANQRRGDCALRHSvsNGEFnlGENIYWGYGANWSPADAVVAWASEKRFY 133
Cdd:cd05381   3 DFLDAHNQARAAVGVPPLVWDDTLAAYAQKYANQRRGDCSLVHS--NGPY--GENLFWGSGDNWSPADAVKSWVDEKPYY 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15235992 134 HYGSNTCDAGQMCGHYTQIVWKSTRRVGCARVVCDN-GGIFMTCNYDPPGNYIGQKPY 190
Cdd:cd05381  79 DYASNTCVGGKMCGHYTQVVWRNSTRLGCARVVCDNnGGTFVICNYDPPGNYIGERPY 136

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235992  59 HNLVRAARFEPPLIWDRRLQNYAQGWANQRRGDCALRHSvsNGEFnlGENIYWGYGanwSPADAVVAWASEKRFYHYgsN 138
Cdd:cd05384  10 HNKKRALHGTQPLTWNDTLAEYAQDYADSYDCSGNLVHS--GGPY--GENLALGYS---SGAAAVDAWYDEISDYDY--S 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 15235992 139 TCDAGQMCGHYTQIVWKSTRRVGCARVVCDNG-GIFMTCNYDPPGNYIG 186
Cdd:cd05384  81 NPGFSESTGHFTQLVWKSTTQVGCAYKDCGGAwGLYIVCEYDPAGNVIG 129

CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain of glioma pathogenesis-related protein 1 and similar proteins; Glioma pathogenesis-related protein 1 (GLIPR1) is also called related to testes-specific, vespid, and pathogenesis protein 1 (RTVP-1). The GLIPR1 gene has been identified as a p53 target gene and was shown to be methylated and down-regulated in prostate cancer. It is a novel broad-spectrum tumor suppressor whose proapoptotic properties are exerted in part through ROS-JNK signaling. GLIPR1 is composed of a signal peptide that directs its secretion, a CAP domain, and a transmembrane domain. 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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235992  59 HNLVRAaRFEPP------LIWDRRLQNYAQGWANQrrgdCALRHSVSNGEFN--------LGENIYWGYGANWSPADAVV 124
Cdd:cd05385  10 HNELRS-KVSPPaanmryMSWDKALAKTARAWARK----CKFSHNICLKEPGkchpnfttLGENIWLGSIFSFSVESAIT 84

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15235992 125 AWASEKRFYHYGSNTCDagQMCGHYTQIVWKSTRRVGCARVVCDNGGIFMT--------CNYDPPG 182
Cdd:cd05385  85 SWYNEVKDYNFKTNSCS--RVCGHYTQVVWADSYKVGCAVHVCPNGGGFFSgsssaifvCNYGPAG 148

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235992  54 QFLFRHNLVRA-----ARFEPPLIWDRRLQNYAQGWANQrrgdCALRHSVSNGEFNLGENIYWG-YGANWSpaDAVVAWA 127
Cdd:cd00168   3 EILDLHNSYRSsvsppASNMPLMAWDQELADVAIGYAKD----CIFSHSSPTSRQLAGENIAASsYDMDGV--AALQAWH 76

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 15235992 128 SEKRFYHYGSNTCDAGQMCGHYTQIVWKSTRRVGCARVVCDNGGIFMTCNY 178
Cdd:cd00168  77 NEIKNYNFGTAQPGFNSGTGHYTQMVWEKTTKLGCGVADCSDNSKFVVCNY 127

CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain of cysteine-rich secretory proteins; Cysteine-rich secretory proteins (CRISPs) are two-domain proteins with an evolutionary diverse and structurally conserved N-terminal CAP domain and a C-terminal cysteine-rich domain, which is comprised of a hinge and an ICR (ion channel regulator) region. CRISPs are involved in response to pathogens, fertilization, and sperm maturation. One member, Tex31 from the venom duct of Conus textile, has been shown to possess proteolytic activity sensitive to serine protease inhibitors. CRISP-1 has been shown to mediate gamete fusion by binding to the egg surface. Other members of the CRISP family secreted in the testis (CRISP2), epididymis (CRISP3-4), or during ejaculation (CRISP3), are also involved in sperm-egg interaction, supporting the existence of a functional redundancy and cooperation between homolog proteins ensuring the success of fertilization. The wider family of CAP domain containing proteins includes plant pathogenesis-related protein 1 (PR-1) and allergen 5 from vespid venom, among others.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235992  73 WDRRLQNYAQGWANQrrgdCALRHSVSN----GEFNLGENIYWG-YGANWSpaDAVVAWASEKRFYHYGSNTCDAGQMCG 147
Cdd:cd05383  29 WNPEAAENAQRWANR----CNFTHSPPNgrtiPGIRCGENIFMSsYPASWS--EVIQAWYDEYKDFKYGVGAKPPGSVTG 102

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 15235992 148 HYTQIVWKSTRRVGCARVVCDNGG---IFMTCNYDP 180
Cdd:cd05383 103 HYTQVVWYSSYLVGCAVAYCPSQGslkYFYVCQYCP 138

CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain of cysteine-rich secretory protein LCCL domain-containing 2; Cysteine-rich secretory protein LCCL domain-containing 2 (CRISPLD2) is also called cysteine-rich secretory protein 11 (CRSIP-11), LCCL domain-containing cysteine-rich secretory protein 2 (LCRISP2), or CAP and LCCL domain containing protein 2 (CAPLD2). It plays a role in the etiology of NSCLP (non-syndromic cleft lip with or without cleft palate). It is required for neural crest cell migration and cell viability during craniofacial development. The CRISPLD2 gene has been identified a glucocorticoid responsive gene that modulates cytokine function in airway smooth muscle cells. 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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235992  71 LIWDRRLQNYAQGWANQrrgdCALRHSVSNGEFNLGENIYWGYGANWSPADAVVAWASEKRFYHYG-SNTCD-------A 142
Cdd:cd18816  25 MTWDDELERSAEAWAQQ----CIWEHGPTSLLPSIGQNLAVHWGRYRSPAFHVQSWYDEVKDYTYPyPHECNpwcpercS 100

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 15235992 143 GQMCGHYTQIVWKSTRRVGCARVVCD---------NGGIFMTCNY 178
Cdd:cd18816 101 GPMCTHYTQIVWATTNKVGCAVNVCRrmnvwgeiwENAVYLVCNY 145

CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain of peptidase inhibitor 15 and similar proteins; This family is composed of peptidase inhibitor 15 (PI15), peptidase inhibitor R3HDML, cysteine-rich secretory protein LCCL domain-containing 1 (CRISPLD1), and cysteine-rich secretory protein LCCL domain-containing 2 (CRISPLD2). PI15 is a serine protease inhibitor which displays weak inhibitory activity against trypsin and may play a role in facial patterning during embryonic development. The PI15 gene is a candidate gene for abdominal aortic internal elastic lamina ruptures in the rat. R3HDML is a putative serine protease inhibitor, whose gene may be associated with clinical dimensions of schizophrenia. CRISPLD1 may play a role in NSCLP (nonsyndromic cleft lip with or without cleft palate) through the interaction with CRISPLD2 and folate pathway genes. plays a role in the etiology of NSCLP and is required for neural crest cell migration and cell viability during craniofacial development. 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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235992  59 HNLVRAARFEPP-----LIWDRRLQNYAQGWANQrrgdCALRHSVSNGEFNLGENIYWGYGANWSPADAVVAWASEKRFY 133
Cdd:cd18812   8 HNKLRGQVYPPAanmeyMVWDKELARSAEAWATQ----CIWEHGPSSLLRSIGQNLSAHWGRYRSPVFLVKSWYDEVKDY 83

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15235992 134 HY-GSNTCD-------AGQMCGHYTQIVWKSTRRVGCARVVCDN---------GGIFMTCNY 178
Cdd:cd18812  84 LFpYPRDCNphcpwrcSGPMCTHYTQMVWATSNRIGCAIHTCSNmnvwgnvwhRAVYLVCNY 145

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];

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235992  54 QFLFRHNLVRAARFEPPLIWDRRLQNYAQGWANQ--RRGDcaLRHSVSNG------------EFNL-GENIYWGYGanwS 118
Cdd:COG2340  23 EVLELVNAYRAAAGLPPLTWDPRLTAAARAHAQDmaENGY--FSHTGPDGsspfdrlkaagySYRAaGENIAAGYS---T 97

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15235992 119 PADAVVAW-ASEkrfyhygsntcdagqmcGHYTQIVWKSTRRVGCARVVCDNGGIFMTCNY 178
Cdd:COG2340  98 AEEAVDGWmNSP-----------------GHRANILNPDFTEIGVGVAYGGDGGVYWTQVF 141

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235992  60 NLVRAARFEPPLIWDRRLQNYAQGWAN-------------QRRGDCALRHSVSNGefNLGENIYWGYGanwSPADAVVAW 126
Cdd:cd05379   9 NEYRAKAGLPPLSWDPRLEKAAQDHAEdmaangyfshtgpDGSSDRAARAGYWYR--GAGENIAYGQG---SAEEAVNQW 83

                ...
gi 15235992 127 ASE 129
Cdd:cd05379  84 INS 86