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Conserved domains on  [gi|1278708287|gb|PJC08611|]
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hypothetical protein CO068_00125 [Flavobacteriaceae bacterium CG_4_9_14_0_8_um_filter_34_30]

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 ...
 59-178 4.93e-23

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: 88.90  E-value: 4.93e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278708287  59 AMENDLFERVNQYRISLGKAPLERNTDADNQASEHTIYMVEKNNINHDFLQQRTAF----FLNLGFVSLKENVASGYTNA 134
Cdd:COG2340    19 ALEQEVLELVNAYRAAAGLPPLTWDPRLTAAARAHAQDMAENGYFSHTGPDGSSPFdrlkAAGYSYRAAGENIAAGYSTA 98

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1278708287 135 QTLLDAWLQSESHRFAIEADGV-ATGISVLKNEAGIQFITQIYLK 178
Cdd:COG2340    99 EEAVDGWMNSPGHRANILNPDFtEIGVGVAYGGDGGVYWTQVFGR 143
 
Name Accession Description Interval E-value
YkwD COG2340
Spore germination protein YkwD and related proteins with CAP (CSP/antigen 5/PR1) domain [Cell ...
 59-178 4.93e-23

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: 88.90  E-value: 4.93e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278708287  59 AMENDLFERVNQYRISLGKAPLERNTDADNQASEHTIYMVEKNNINHDFLQQRTAF----FLNLGFVSLKENVASGYTNA 134
Cdd:COG2340    19 ALEQEVLELVNAYRAAAGLPPLTWDPRLTAAARAHAQDMAENGYFSHTGPDGSSPFdrlkAAGYSYRAAGENIAAGYSTA 98

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1278708287 135 QTLLDAWLQSESHRFAIEADGV-ATGISVLKNEAGIQFITQIYLK 178
Cdd:COG2340    99 EEAVDGWMNSPGHRANILNPDFtEIGVGVAYGGDGGVYWTQVFGR 143
CAP_bacterial cd05379
Bacterial CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 ...
 61-176 2.91e-21

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: 83.58  E-value: 2.91e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278708287  61 ENDLFERVNQYRISLGKAPLERNTDADNQASEHTIYMVEKNNINHDFLQQRTAFFLNLGFVSLK--ENVASGYTNAQTLL 138
Cdd:cd05379     1 EQEVLELINEYRAKAGLPPLSWDPRLEKAAQDHAEDMAANGYFSHTGPDGSSDRAARAGYWYRGagENIAYGQGSAEEAV 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1278708287 139 DAWLQSESHRFAIEADG-VATGISVLKNEAGIQFITQIY 176
Cdd:cd05379    81 NQWINSPGHRANILDPDfTEIGVGVAYNSSGGTYWTQVF 119
CAP pfam00188
Cysteine-rich secretory protein family; This is a large family of cysteine-rich secretory ...
 65-176 1.50e-09

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: 52.98  E-value: 1.50e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278708287  65 FERVNQYRISLGKAPLERNTDADNQASEHTIYMVEKNNINHDFLQQRTafFLNLGFVSLKENVASGYTNAQTLLDAWLQS 144
Cdd:pfam00188   1 LDLHNEYRAAAGLPPLSWDNELAAAAQDHAKYCADNGSHNHRSPYGGN--IYARVVAAGYALGDAGPDSAEDAVDGWYDS 78

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1278708287 145 E-----SHRFAIEADGV-ATGISVLKNEAGIQFI-TQIY 176
Cdd:pfam00188  79 PgtyncGHRTNLLWPKStKVGCAVAKCGDGGTYYfVCNY 117
 
Name Accession Description Interval E-value
YkwD COG2340
Spore germination protein YkwD and related proteins with CAP (CSP/antigen 5/PR1) domain [Cell ...
 59-178 4.93e-23

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: 88.90  E-value: 4.93e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278708287  59 AMENDLFERVNQYRISLGKAPLERNTDADNQASEHTIYMVEKNNINHDFLQQRTAF----FLNLGFVSLKENVASGYTNA 134
Cdd:COG2340    19 ALEQEVLELVNAYRAAAGLPPLTWDPRLTAAARAHAQDMAENGYFSHTGPDGSSPFdrlkAAGYSYRAAGENIAAGYSTA 98

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1278708287 135 QTLLDAWLQSESHRFAIEADGV-ATGISVLKNEAGIQFITQIYLK 178
Cdd:COG2340    99 EEAVDGWMNSPGHRANILNPDFtEIGVGVAYGGDGGVYWTQVFGR 143
CAP_bacterial cd05379
Bacterial CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 ...
 61-176 2.91e-21

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: 83.58  E-value: 2.91e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278708287  61 ENDLFERVNQYRISLGKAPLERNTDADNQASEHTIYMVEKNNINHDFLQQRTAFFLNLGFVSLK--ENVASGYTNAQTLL 138
Cdd:cd05379     1 EQEVLELINEYRAKAGLPPLSWDPRLEKAAQDHAEDMAANGYFSHTGPDGSSDRAARAGYWYRGagENIAYGQGSAEEAV 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1278708287 139 DAWLQSESHRFAIEADG-VATGISVLKNEAGIQFITQIY 176
Cdd:cd05379    81 NQWINSPGHRANILDPDfTEIGVGVAYNSSGGTYWTQVF 119
CAP pfam00188
Cysteine-rich secretory protein family; This is a large family of cysteine-rich secretory ...
 65-176 1.50e-09

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: 52.98  E-value: 1.50e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278708287  65 FERVNQYRISLGKAPLERNTDADNQASEHTIYMVEKNNINHDFLQQRTafFLNLGFVSLKENVASGYTNAQTLLDAWLQS 144
Cdd:pfam00188   1 LDLHNEYRAAAGLPPLSWDNELAAAAQDHAKYCADNGSHNHRSPYGGN--IYARVVAAGYALGDAGPDSAEDAVDGWYDS 78

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1278708287 145 E-----SHRFAIEADGV-ATGISVLKNEAGIQFI-TQIY 176
Cdd:pfam00188  79 PgtyncGHRTNLLWPKStKVGCAVAKCGDGGTYYfVCNY 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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