NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1939339774|ref|WP_196465357|]
View 

CAP domain-containing protein [Streptomyces spinoverrucosus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 314-452 1.30e-60

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: 194.45  E-value: 1.30e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939339774 314 TAVWARPLAPADLTRTAADVIDLTNRERTRAGLPPLSSDPALARAAQAHSADMVARDFYSHTAPDGSQPWDRAAAAGSTR 393
Cdd:COG2340     5 LLLAAAAAAPAALSALEQEVLELVNAYRAAAGLPPLTWDPRLTAAARAHAQDMAENGYFSHTGPDGSSPFDRLKAAGYSY 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1939339774 394 RSIGENIACGQRSPAEVVTGWMNSPGHRANILKPGFTHIGIGFAGGGRAGTYWTQLFGG 452
Cdd:COG2340    85 RAAGENIAAGYSTAEEAVDGWMNSPGHRANILNPDFTEIGVGVAYGGDGGVYWTQVFGR 143
TerD_like cd06974
Uncharacterized proteins involved in stress response, similar to tellurium resistance terD; ...
 22-154 2.72e-33

Uncharacterized proteins involved in stress response, similar to tellurium resistance terD; Tellurium resistance terD like proteins. This family is composed of uncharacterized proteins involved in stress response, such as the tellurium resistance proteins, chemical-damaging agent resistance proteins, and general stress proteins from a variety of organisms. The tellurium resistance proteins are homologous terA,-D,-E,-F,-Z,-X gene products, which confer tellurium resistance mediated by plasmids. Currently, the biochemical mechanism of tellurium resistance remains unknown. The family also contains several ter gene homologues, YceC, YceD, YceE, for which there is no clear evidence for any involvement in the tellurium resistance. A putative cAMP-binding protin CABP1 shows a significant similarity to the terD protein and is also included in this family.


:

Pssm-ID: 132992  Cd Length: 162  Bit Score: 123.18  E-value: 2.72e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939339774  22 PGPFDMSALITDDDGKVRGDSDFVFYNQPSAP-GAV-LRGD----------TLTVDPTRLRAGATRVTVVVSpADPGTPL 89
Cdd:cd06974    18 GIDLDLSAFLLDADGKVRGDADVVFYNQLSSPdGAVrLSGDnrtggdgddeTITVDLDRLPPDIRRIVFTVT-IYEGQPF 96

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1939339774  90 GRLPVPTLFVTDPGGRH-LARFTPPRPGQETVLLLAELYRRGAGWKVRALGQGYADGLAGLARDFG 154
Cdd:cd06974    97 GQVENAFVRLVDAGGNTeLARYDLTEDSGETALILAELYRRNGEWKFRAVGQGFNGGLAALATHYG 162
YkwD COG2340
Spore germination protein YkwD and related proteins with CAP (CSP/antigen 5/PR1) domain [Cell ...
 202-320 3.06e-27

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: 106.24  E-value: 3.06e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939339774 202 LINPARAQAGSPPVSLDPRLTTAAHQHASAMAAAGQLGVESRDGVAVYQRVTATGFTYITIGEHLVSGPRTPTEFIDYCL 281
Cdd:COG2340    27 LVNAYRAAAGLPPLTWDPRLTAAARAHAQDMAENGYFSHTGPDGSSPFDRLKAAGYSYRAAGENIAAGYSTAEEAVDGWM 106

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1939339774 282 RSDGPRRTLLDPAFTHAGLAHANGGrSGDVYWTAVWARP 320
Cdd:COG2340   107 NSPGHRANILNPDFTEIGVGVAYGG-DGGVYWTQVFGRP 144
 
Name Accession Description Interval E-value
YkwD COG2340
Spore germination protein YkwD and related proteins with CAP (CSP/antigen 5/PR1) domain [Cell ...
 314-452 1.30e-60

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: 194.45  E-value: 1.30e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939339774 314 TAVWARPLAPADLTRTAADVIDLTNRERTRAGLPPLSSDPALARAAQAHSADMVARDFYSHTAPDGSQPWDRAAAAGSTR 393
Cdd:COG2340     5 LLLAAAAAAPAALSALEQEVLELVNAYRAAAGLPPLTWDPRLTAAARAHAQDMAENGYFSHTGPDGSSPFDRLKAAGYSY 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1939339774 394 RSIGENIACGQRSPAEVVTGWMNSPGHRANILKPGFTHIGIGFAGGGRAGTYWTQLFGG 452
Cdd:COG2340    85 RAAGENIAAGYSTAEEAVDGWMNSPGHRANILNPDFTEIGVGVAYGGDGGVYWTQVFGR 143
CAP_bacterial cd05379
Bacterial CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 ...
 330-451 3.46e-49

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: 163.70  E-value: 3.46e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939339774 330 AADVIDLTNRERTRAGLPPLSSDPALARAAQAHSADMVARDFYSHTAPDGSQpwDRAAAAGSTRRSIGENIACGQRSPAE 409
Cdd:cd05379     1 EQEVLELINEYRAKAGLPPLSWDPRLEKAAQDHAEDMAANGYFSHTGPDGSS--DRAARAGYWYRGAGENIAYGQGSAEE 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1939339774 410 VVTGWMNSPGHRANILKPGFTHIGIGFAGGGRAGTYWTQLFG 451
Cdd:cd05379    79 AVNQWINSPGHRANILDPDFTEIGVGVAYNSSGGTYWTQVFG 120
spore_YkwD TIGR02909
uncharacterized protein, YkwD family; Members of this protein family represent a subset of ...
 333-452 3.92e-46

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: 156.05  E-value: 3.92e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939339774 333 VIDLTNRERTRAGLPPLSSDPALARAAQAHSADMVARDFYSHTAPDGSQPWDRAAAAGSTRRSIGENIACGQRSPAEVVT 412
Cdd:TIGR02909   8 VVELVNAERAKNGLKPLKADPELSKVARLKSEDMRDKNYFSHTSPTYGSPFDMMKKFGISYRMAGENIAYGNSTVEAVHN 87

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1939339774 413 GWMNSPGHRANILKPGFTHIGIGFAGGGRAGTYWTQLFGG 452
Cdd:TIGR02909  88 AWMNSPGHRANILNPNYTEIGVGYVEGGSGGIYWTQMFIG 127
TerD_like cd06974
Uncharacterized proteins involved in stress response, similar to tellurium resistance terD; ...
 22-154 2.72e-33

Uncharacterized proteins involved in stress response, similar to tellurium resistance terD; Tellurium resistance terD like proteins. This family is composed of uncharacterized proteins involved in stress response, such as the tellurium resistance proteins, chemical-damaging agent resistance proteins, and general stress proteins from a variety of organisms. The tellurium resistance proteins are homologous terA,-D,-E,-F,-Z,-X gene products, which confer tellurium resistance mediated by plasmids. Currently, the biochemical mechanism of tellurium resistance remains unknown. The family also contains several ter gene homologues, YceC, YceD, YceE, for which there is no clear evidence for any involvement in the tellurium resistance. A putative cAMP-binding protin CABP1 shows a significant similarity to the terD protein and is also included in this family.


Pssm-ID: 132992  Cd Length: 162  Bit Score: 123.18  E-value: 2.72e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939339774  22 PGPFDMSALITDDDGKVRGDSDFVFYNQPSAP-GAV-LRGD----------TLTVDPTRLRAGATRVTVVVSpADPGTPL 89
Cdd:cd06974    18 GIDLDLSAFLLDADGKVRGDADVVFYNQLSSPdGAVrLSGDnrtggdgddeTITVDLDRLPPDIRRIVFTVT-IYEGQPF 96

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1939339774  90 GRLPVPTLFVTDPGGRH-LARFTPPRPGQETVLLLAELYRRGAGWKVRALGQGYADGLAGLARDFG 154
Cdd:cd06974    97 GQVENAFVRLVDAGGNTeLARYDLTEDSGETALILAELYRRNGEWKFRAVGQGFNGGLAALATHYG 162
TerD pfam02342
TerD domain; The TerD domain is found in TerD family proteins that include the paralogous TerD, ...
 1-153 2.85e-32

TerD domain; The TerD domain is found in TerD family proteins that include the paralogous TerD, TerA, TerE, TerF and TerZ proteins It is found in a stress response operon with TerB and TerC. TerD has a maximum of two calcium-binding sites depending on the conservation of aspartates. It has various fusions to nuclease domains, RNA binding domains, ubiquitin related domains, and metal binding domains. The ter gene products lie at the centre of membrane-linked metal recognition complexes with regulatory ramifications encompassing phosphorylation-dependent signal transduction, RNA-dependent regulation, biosynthesis of nucleoside-like metabolites and DNA processing linked to novel pathways.


Pssm-ID: 426730  Cd Length: 187  Bit Score: 121.07  E-value: 2.85e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939339774   1 MS-ELLPGGNLPLPGGA--LT-VRV----------PGPFDM--SALITDDDGKVRGDSDFVFYNQPSAP-GAV-LRGDTL 62
Cdd:pfam02342   1 MAiSLQKGQNISLTKEApgLTkVMVglgwdvnktgGADFDLdaSAFLLGANGKVRSDEDFVFYNNLKSPdGSVrHLGDNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939339774  63 T-----------VDPTRLRAGATRVTVVVS---PADPGTPLGRlpVPTLFVT---DPGGRHLARFTPPRPG-QETVLLLA 124
Cdd:pfam02342  81 TgegdgddeqieVDLSKVPADVEKIVFVVTiydAEARRQNFGQ--VRNAYIRvvdAATGEELARYDLSEDFsGETALIFG 158

                         170       180
                  ....*....|....*....|....*....
gi 1939339774 125 ELYRRGAGWKVRALGQGYADGLAGLARDF 153
Cdd:pfam02342 159 ELYRHGGEWKFRAVGQGYAGGLAGLATDY 187
CAP pfam00188
Cysteine-rich secretory protein family; This is a large family of cysteine-rich secretory ...
 334-450 1.39e-28

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: 108.83  E-value: 1.39e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939339774 334 IDLTNRERTRAGLPPLSSDPALARAAQAHSADMVARDFYSHTAPDGSQPWDRAAAAGStrrsigENIACGQRSPAEVVTG 413
Cdd:pfam00188   1 LDLHNEYRAAAGLPPLSWDNELAAAAQDHAKYCADNGSHNHRSPYGGNIYARVVAAGY------ALGDAGPDSAEDAVDG 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1939339774 414 WMNSP-----GHRANILKPGFTHIGIGFA-GGGRAGTYWTQLF 450
Cdd:pfam00188  75 WYDSPgtyncGHRTNLLWPKSTKVGCAVAkCGDGGTYYFVCNY 117
TerZ COG2310
Stress response protein SCP2 [Signal transduction mechanisms];
1-153 5.66e-28

Stress response protein SCP2 [Signal transduction mechanisms];


Pssm-ID: 441884  Cd Length: 187  Bit Score: 109.49  E-value: 5.66e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939339774   1 MS-ELLPGGNLPLPGGA--LT-VRV----------PGPFDM--SALITDDDGKVRGDSDFVFYNQPSAP-GAV-LRGDTL 62
Cdd:COG2310     1 MAiSLQKGQNISLTKEApgLTkVRVglgwdpaktdGGDFDLdaSAFLLDANGKVRSDEDFVFYNNLKSPdGSVrHTGDNR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939339774  63 T-----------VDPTRLRAGATRVTVVVS---PADPGTPLGRlpVPTLF---VTDPGGRHLARFT-PPRPGQETVLLLA 124
Cdd:COG2310    81 TgegdgddeqitVDLSKVPADVEKIVFVVTiydAEARGQNFGQ--VSNAFirvVDAATGEELARYDlSEDFSGETAMVFG 158

                         170       180
                  ....*....|....*....|....*....
gi 1939339774 125 ELYRRGAGWKVRALGQGYADGLAGLARDF 153
Cdd:COG2310   159 ELYRHGGEWKFRAVGQGYNGGLAGLATDY 187
YkwD COG2340
Spore germination protein YkwD and related proteins with CAP (CSP/antigen 5/PR1) domain [Cell ...
 202-320 3.06e-27

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: 106.24  E-value: 3.06e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939339774 202 LINPARAQAGSPPVSLDPRLTTAAHQHASAMAAAGQLGVESRDGVAVYQRVTATGFTYITIGEHLVSGPRTPTEFIDYCL 281
Cdd:COG2340    27 LVNAYRAAAGLPPLTWDPRLTAAARAHAQDMAENGYFSHTGPDGSSPFDRLKAAGYSYRAAGENIAAGYSTAEEAVDGWM 106

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1939339774 282 RSDGPRRTLLDPAFTHAGLAHANGGrSGDVYWTAVWARP 320
Cdd:COG2340   107 NSPGHRANILNPDFTEIGVGVAYGG-DGGVYWTQVFGRP 144
CAP_bacterial cd05379
Bacterial CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 ...
 202-318 2.45e-24

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: 97.45  E-value: 2.45e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939339774 202 LINPARAQAGSPPVSLDPRLTTAAHQHASAMAAAGQLGVESRDGVAvyQRVTATGFTYITIGEHLVSGPRTPTEFIDYCL 281
Cdd:cd05379     7 LINEYRAKAGLPPLSWDPRLEKAAQDHAEDMAANGYFSHTGPDGSS--DRAARAGYWYRGAGENIAYGQGSAEEAVNQWI 84

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1939339774 282 RSDGPRRTLLDPAFTHAGLAHANGGrSGDVYWTAVWA 318
Cdd:cd05379    85 NSPGHRANILDPDFTEIGVGVAYNS-SGGTYWTQVFG 120
CAP pfam00188
Cysteine-rich secretory protein family; This is a large family of cysteine-rich secretory ...
 202-316 1.30e-14

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: 69.92  E-value: 1.30e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939339774 202 LINPARAQAGSPPVSLDPRLTTAAHQHASAMAAAGQLGVESRDGVAVYQRVTATGFTYItigehlVSGPRTPTEFIDYCL 281
Cdd:pfam00188   3 LHNEYRAAAGLPPLSWDNELAAAAQDHAKYCADNGSHNHRSPYGGNIYARVVAAGYALG------DAGPDSAEDAVDGWY 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1939339774 282 RSDGP-----RRTLLDPAFTHAGLAHANGGRSGDVYWTAV 316
Cdd:pfam00188  77 DSPGTyncghRTNLLWPKSTKVGCAVAKCGDGGTYYFVCN 116
 
Name Accession Description Interval E-value
YkwD COG2340
Spore germination protein YkwD and related proteins with CAP (CSP/antigen 5/PR1) domain [Cell ...
 314-452 1.30e-60

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: 194.45  E-value: 1.30e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939339774 314 TAVWARPLAPADLTRTAADVIDLTNRERTRAGLPPLSSDPALARAAQAHSADMVARDFYSHTAPDGSQPWDRAAAAGSTR 393
Cdd:COG2340     5 LLLAAAAAAPAALSALEQEVLELVNAYRAAAGLPPLTWDPRLTAAARAHAQDMAENGYFSHTGPDGSSPFDRLKAAGYSY 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1939339774 394 RSIGENIACGQRSPAEVVTGWMNSPGHRANILKPGFTHIGIGFAGGGRAGTYWTQLFGG 452
Cdd:COG2340    85 RAAGENIAAGYSTAEEAVDGWMNSPGHRANILNPDFTEIGVGVAYGGDGGVYWTQVFGR 143
CAP_bacterial cd05379
Bacterial CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 ...
 330-451 3.46e-49

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: 163.70  E-value: 3.46e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939339774 330 AADVIDLTNRERTRAGLPPLSSDPALARAAQAHSADMVARDFYSHTAPDGSQpwDRAAAAGSTRRSIGENIACGQRSPAE 409
Cdd:cd05379     1 EQEVLELINEYRAKAGLPPLSWDPRLEKAAQDHAEDMAANGYFSHTGPDGSS--DRAARAGYWYRGAGENIAYGQGSAEE 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1939339774 410 VVTGWMNSPGHRANILKPGFTHIGIGFAGGGRAGTYWTQLFG 451
Cdd:cd05379    79 AVNQWINSPGHRANILDPDFTEIGVGVAYNSSGGTYWTQVFG 120
spore_YkwD TIGR02909
uncharacterized protein, YkwD family; Members of this protein family represent a subset of ...
 333-452 3.92e-46

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: 156.05  E-value: 3.92e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939339774 333 VIDLTNRERTRAGLPPLSSDPALARAAQAHSADMVARDFYSHTAPDGSQPWDRAAAAGSTRRSIGENIACGQRSPAEVVT 412
Cdd:TIGR02909   8 VVELVNAERAKNGLKPLKADPELSKVARLKSEDMRDKNYFSHTSPTYGSPFDMMKKFGISYRMAGENIAYGNSTVEAVHN 87

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1939339774 413 GWMNSPGHRANILKPGFTHIGIGFAGGGRAGTYWTQLFGG 452
Cdd:TIGR02909  88 AWMNSPGHRANILNPNYTEIGVGYVEGGSGGIYWTQMFIG 127
TerD_like cd06974
Uncharacterized proteins involved in stress response, similar to tellurium resistance terD; ...
 22-154 2.72e-33

Uncharacterized proteins involved in stress response, similar to tellurium resistance terD; Tellurium resistance terD like proteins. This family is composed of uncharacterized proteins involved in stress response, such as the tellurium resistance proteins, chemical-damaging agent resistance proteins, and general stress proteins from a variety of organisms. The tellurium resistance proteins are homologous terA,-D,-E,-F,-Z,-X gene products, which confer tellurium resistance mediated by plasmids. Currently, the biochemical mechanism of tellurium resistance remains unknown. The family also contains several ter gene homologues, YceC, YceD, YceE, for which there is no clear evidence for any involvement in the tellurium resistance. A putative cAMP-binding protin CABP1 shows a significant similarity to the terD protein and is also included in this family.


Pssm-ID: 132992  Cd Length: 162  Bit Score: 123.18  E-value: 2.72e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939339774  22 PGPFDMSALITDDDGKVRGDSDFVFYNQPSAP-GAV-LRGD----------TLTVDPTRLRAGATRVTVVVSpADPGTPL 89
Cdd:cd06974    18 GIDLDLSAFLLDADGKVRGDADVVFYNQLSSPdGAVrLSGDnrtggdgddeTITVDLDRLPPDIRRIVFTVT-IYEGQPF 96

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1939339774  90 GRLPVPTLFVTDPGGRH-LARFTPPRPGQETVLLLAELYRRGAGWKVRALGQGYADGLAGLARDFG 154
Cdd:cd06974    97 GQVENAFVRLVDAGGNTeLARYDLTEDSGETALILAELYRRNGEWKFRAVGQGFNGGLAALATHYG 162
TerD pfam02342
TerD domain; The TerD domain is found in TerD family proteins that include the paralogous TerD, ...
 1-153 2.85e-32

TerD domain; The TerD domain is found in TerD family proteins that include the paralogous TerD, TerA, TerE, TerF and TerZ proteins It is found in a stress response operon with TerB and TerC. TerD has a maximum of two calcium-binding sites depending on the conservation of aspartates. It has various fusions to nuclease domains, RNA binding domains, ubiquitin related domains, and metal binding domains. The ter gene products lie at the centre of membrane-linked metal recognition complexes with regulatory ramifications encompassing phosphorylation-dependent signal transduction, RNA-dependent regulation, biosynthesis of nucleoside-like metabolites and DNA processing linked to novel pathways.


Pssm-ID: 426730  Cd Length: 187  Bit Score: 121.07  E-value: 2.85e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939339774   1 MS-ELLPGGNLPLPGGA--LT-VRV----------PGPFDM--SALITDDDGKVRGDSDFVFYNQPSAP-GAV-LRGDTL 62
Cdd:pfam02342   1 MAiSLQKGQNISLTKEApgLTkVMVglgwdvnktgGADFDLdaSAFLLGANGKVRSDEDFVFYNNLKSPdGSVrHLGDNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939339774  63 T-----------VDPTRLRAGATRVTVVVS---PADPGTPLGRlpVPTLFVT---DPGGRHLARFTPPRPG-QETVLLLA 124
Cdd:pfam02342  81 TgegdgddeqieVDLSKVPADVEKIVFVVTiydAEARRQNFGQ--VRNAYIRvvdAATGEELARYDLSEDFsGETALIFG 158

                         170       180
                  ....*....|....*....|....*....
gi 1939339774 125 ELYRRGAGWKVRALGQGYADGLAGLARDF 153
Cdd:pfam02342 159 ELYRHGGEWKFRAVGQGYAGGLAGLATDY 187
CAP pfam00188
Cysteine-rich secretory protein family; This is a large family of cysteine-rich secretory ...
 334-450 1.39e-28

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: 108.83  E-value: 1.39e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939339774 334 IDLTNRERTRAGLPPLSSDPALARAAQAHSADMVARDFYSHTAPDGSQPWDRAAAAGStrrsigENIACGQRSPAEVVTG 413
Cdd:pfam00188   1 LDLHNEYRAAAGLPPLSWDNELAAAAQDHAKYCADNGSHNHRSPYGGNIYARVVAAGY------ALGDAGPDSAEDAVDG 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1939339774 414 WMNSP-----GHRANILKPGFTHIGIGFA-GGGRAGTYWTQLF 450
Cdd:pfam00188  75 WYDSPgtyncGHRTNLLWPKSTKVGCAVAkCGDGGTYYFVCNY 117
TerZ COG2310
Stress response protein SCP2 [Signal transduction mechanisms];
1-153 5.66e-28

Stress response protein SCP2 [Signal transduction mechanisms];


Pssm-ID: 441884  Cd Length: 187  Bit Score: 109.49  E-value: 5.66e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939339774   1 MS-ELLPGGNLPLPGGA--LT-VRV----------PGPFDM--SALITDDDGKVRGDSDFVFYNQPSAP-GAV-LRGDTL 62
Cdd:COG2310     1 MAiSLQKGQNISLTKEApgLTkVRVglgwdpaktdGGDFDLdaSAFLLDANGKVRSDEDFVFYNNLKSPdGSVrHTGDNR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939339774  63 T-----------VDPTRLRAGATRVTVVVS---PADPGTPLGRlpVPTLF---VTDPGGRHLARFT-PPRPGQETVLLLA 124
Cdd:COG2310    81 TgegdgddeqitVDLSKVPADVEKIVFVVTiydAEARGQNFGQ--VSNAFirvVDAATGEELARYDlSEDFSGETAMVFG 158

                         170       180
                  ....*....|....*....|....*....
gi 1939339774 125 ELYRRGAGWKVRALGQGYADGLAGLARDF 153
Cdd:COG2310   159 ELYRHGGEWKFRAVGQGYNGGLAGLATDY 187
YkwD COG2340
Spore germination protein YkwD and related proteins with CAP (CSP/antigen 5/PR1) domain [Cell ...
 202-320 3.06e-27

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: 106.24  E-value: 3.06e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939339774 202 LINPARAQAGSPPVSLDPRLTTAAHQHASAMAAAGQLGVESRDGVAVYQRVTATGFTYITIGEHLVSGPRTPTEFIDYCL 281
Cdd:COG2340    27 LVNAYRAAAGLPPLTWDPRLTAAARAHAQDMAENGYFSHTGPDGSSPFDRLKAAGYSYRAAGENIAAGYSTAEEAVDGWM 106

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1939339774 282 RSDGPRRTLLDPAFTHAGLAHANGGrSGDVYWTAVWARP 320
Cdd:COG2340   107 NSPGHRANILNPDFTEIGVGVAYGG-DGGVYWTQVFGRP 144
CAP_bacterial cd05379
Bacterial CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 ...
 202-318 2.45e-24

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: 97.45  E-value: 2.45e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939339774 202 LINPARAQAGSPPVSLDPRLTTAAHQHASAMAAAGQLGVESRDGVAvyQRVTATGFTYITIGEHLVSGPRTPTEFIDYCL 281
Cdd:cd05379     7 LINEYRAKAGLPPLSWDPRLEKAAQDHAEDMAANGYFSHTGPDGSS--DRAARAGYWYRGAGENIAYGQGSAEEAVNQWI 84

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1939339774 282 RSDGPRRTLLDPAFTHAGLAHANGGrSGDVYWTAVWA 318
Cdd:cd05379    85 NSPGHRANILDPDFTEIGVGVAYNS-SGGTYWTQVFG 120
CAP pfam00188
Cysteine-rich secretory protein family; This is a large family of cysteine-rich secretory ...
 202-316 1.30e-14

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: 69.92  E-value: 1.30e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939339774 202 LINPARAQAGSPPVSLDPRLTTAAHQHASAMAAAGQLGVESRDGVAVYQRVTATGFTYItigehlVSGPRTPTEFIDYCL 281
Cdd:pfam00188   3 LHNEYRAAAGLPPLSWDNELAAAAQDHAKYCADNGSHNHRSPYGGNIYARVVAAGYALG------DAGPDSAEDAVDGWY 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1939339774 282 RSDGP-----RRTLLDPAFTHAGLAHANGGRSGDVYWTAV 316
Cdd:pfam00188  77 DSPGTyncghRTNLLWPKSTKVGCAVAKCGDGGTYYFVCN 116
CAP_GAPR1-like cd05382
CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain ...
 332-446 6.21e-09

CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain of Golgi-associated plant pathogenesis-related protein 1 and similar proteins; Golgi-associated plant pathogenesis related protein 1 (GAPR1), also called Golgi-associated PR-1 protein or glioma pathogenesis-related protein 2 (GLIPR-2), forms amyloid-like fibrils in the presence of liposomes containing acidic phospholipids. It has been identified in mice as an up-regulated protein in kidney fibrosis, and is involved in epithelial to mesenchymal transition and in generating a pool of myofibroblasts contributing to fibrosis. 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: 349401  Cd Length: 132  Bit Score: 54.14  E-value: 6.21e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939339774 332 DVIDLTNRERTRAGLPPLSSDPALARAAQAHSADMVARDFYSHtapdgsqpwdraaaagSTRRSIGENIAC-----GQRS 406
Cdd:cd05382     5 ECLKAHNEYRALHGAPPLKLDKELSKEAQKWAEKLASSGTLQH----------------SSPSSYGENLAYfsgsgYDLT 68

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1939339774 407 PAEVVTGWMNSPGHrANILKPGF---------------THIGIGFAGGGRAGTYW 446
Cdd:cd05382    69 GEEAVDSWYNEIKN-YNFNKPGFqsgtghftqvvwkssTELGVGVAKSKDGCVYV 122
CAP cd00168
CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain ...
 333-451 1.54e-05

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: 44.15  E-value: 1.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939339774 333 VIDLTNRERTR-----AGLPPLSSDPALARAAQAHSADMVardfYSHTAPDGsqpwdraaaagstRRSIGENIACGQRSP 407
Cdd:cd00168     4 ILDLHNSYRSSvsppaSNMPLMAWDQELADVAIGYAKDCI----FSHSSPTS-------------RQLAGENIAASSYDM 66

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1939339774 408 A--EVVTGWMNSP----------------GHRANILKPGFTHIGIGFAGGGRAGTYWTQLFG 451
Cdd:cd00168    67 DgvAALQAWHNEIknynfgtaqpgfnsgtGHYTQMVWEKTTKLGCGVADCSDNSKFVVCNYI 128
CAP_PR-1 cd05381
CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain ...
 330-416 3.06e-03

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: 38.00  E-value: 3.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939339774 330 AADVIDLTNRERTRAGLPPLSSDPALARAAQAHsadmvARDFYSHTAPDGSQPwdraaaagstrrSIGENIACG---QRS 406
Cdd:cd05381     1 PQDFLDAHNQARAAVGVPPLVWDDTLAAYAQKY-----ANQRRGDCSLVHSNG------------PYGENLFWGsgdNWS 63

                          90
                  ....*....|
gi 1939339774 407 PAEVVTGWMN 416
Cdd:cd05381    64 PADAVKSWVD 73
CAP_GAPR1-like cd05382
CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain ...
 207-238 6.77e-03

CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain of Golgi-associated plant pathogenesis-related protein 1 and similar proteins; Golgi-associated plant pathogenesis related protein 1 (GAPR1), also called Golgi-associated PR-1 protein or glioma pathogenesis-related protein 2 (GLIPR-2), forms amyloid-like fibrils in the presence of liposomes containing acidic phospholipids. It has been identified in mice as an up-regulated protein in kidney fibrosis, and is involved in epithelial to mesenchymal transition and in generating a pool of myofibroblasts contributing to fibrosis. 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: 349401  Cd Length: 132  Bit Score: 36.81  E-value: 6.77e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1939339774 207 RAQAGSPPVSLDPRLTTAAHQHASAMAAAGQL 238
Cdd:cd05382    14 RALHGAPPLKLDKELSKEAQKWAEKLASSGTL 45
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH