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Conserved domains on  [gi|753936895|ref|WP_041651319|]
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beta/gamma crystallin-related protein [Marinomonas posidonica]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PFM_crystallin-like cd20232
pore-forming module (PFM) of uncharacterized proteins which have N-terminal crystallin domain ...
 202-352 5.55e-73

pore-forming module (PFM) of uncharacterized proteins which have N-terminal crystallin domain(s), and similar aerolysin-type beta-barrel pore-forming proteins; Many proteins belonging to this group have N-terminal crystallin (beta/gamma crystallins) domain(s). Members of this group belong to the aerolysin family of beta-pore-forming proteins (beta-PFPs). PFPs are generally secreted as water-soluble monomers, which upon binding to target lipid membranes, oligomerize and form transmembrane pores harmful to cells. Beta-PFPs form pores by transmembrane beta-barrels. Aerolysin-type beta-PFPs are believed to use an amphipathic beta-hairpin to form the beta-barrel, are found in all kingdoms of life and many are bacterial toxins. In addition to having a role in microbial infection, they have potential as biotechnological sensors and delivery systems. They share a similar monomeric architecture, with a variable membrane-binding domain and a structurally conserved pore-forming region. A significant portion of the monomeric subunit structure is re-organized to form the pore. Oligomers formed by members of the aerolysin family include: hepta- (aerolysin), octa- (Dln1), and nonameric oligomers (lysenin and monalysin).


:

Pssm-ID: 380802 [Multi-domain]  Cd Length: 151  Bit Score: 223.21  E-value: 5.55e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753936895 202 RPISISGSCISKSSVDQVYTVELKKTLSSSISRSWSDSTMNGIEVSETASMTVEGVAVSGTISTTISRQLENTFTVGEEE 281
Cdd:cd20232    1 EPIGISSSTQNGSDIEQVATLTLERELSKSTTRSFSESTLIGIEVSTTASVGVSAGPVSAEVEQTVTSTLENTFTIGKEE 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 753936895 282 ITSETAEYGQSVSITLPPNHRCEASIELTLKKYKVEANYIYRLKGSELKGKQKVTFEVDDYQAGEVKIETR 352
Cdd:cd20232   81 TKSETITFSKSVNVTIPPGNIGEAVMTLTPKKYKVEAIYTFRLKGTELKFKQKVIIEVDDYQTGEVKIEKF 151
Crystall super family cl02528
Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity ...
 99-179 8.45e-09

Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity between them is very low.


The actual alignment was detected with superfamily member smart00247:

Pssm-ID: 470604  Cd Length: 82  Bit Score: 51.74  E-value: 8.45e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753936895    99 VRFYEHANFTGfeQNLagteEVTE-YPS--PFLMNDSLTSLKVPEGCsVVLYKDTDFRGSSLELGAGE--HYLGHYGFND 173
Cdd:smart00247   2 ITLYEDENFQG--RSY----ELSDdCPSlqDYGSRDNVSSVRVESGC-WVLYEQPNYRGRQYVLEPGEypDYQEWGGFND 74


                   ....*.
gi 753936895   174 LVSSMK 179
Cdd:smart00247  75 QISSIR 80
Crystall super family cl02528
Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity ...
 5-87 1.10e-07

Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity between them is very low.


The actual alignment was detected with superfamily member smart00247:

Pssm-ID: 470604  Cd Length: 82  Bit Score: 48.66  E-value: 1.10e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753936895     5 LYKDANFNGTRRDFEEgEYPSIGD--IDNKVSSLKVGAGWYVeLYPGTGFRGDKVVLFTGEYgilpstISNGQISIWNDQ 82
Cdd:smart00247   4 LYEDENFQGRSYELSD-DCPSLQDygSRDNVSSVRVESGCWV-LYEQPNYRGRQYVLEPGEY------PDYQEWGGFNDQ 75


                   ....*
gi 753936895    83 ISSMK 87
Cdd:smart00247  76 ISSIR 80
 
Name Accession Description Interval E-value
PFM_crystallin-like cd20232
pore-forming module (PFM) of uncharacterized proteins which have N-terminal crystallin domain ...
 202-352 5.55e-73

pore-forming module (PFM) of uncharacterized proteins which have N-terminal crystallin domain(s), and similar aerolysin-type beta-barrel pore-forming proteins; Many proteins belonging to this group have N-terminal crystallin (beta/gamma crystallins) domain(s). Members of this group belong to the aerolysin family of beta-pore-forming proteins (beta-PFPs). PFPs are generally secreted as water-soluble monomers, which upon binding to target lipid membranes, oligomerize and form transmembrane pores harmful to cells. Beta-PFPs form pores by transmembrane beta-barrels. Aerolysin-type beta-PFPs are believed to use an amphipathic beta-hairpin to form the beta-barrel, are found in all kingdoms of life and many are bacterial toxins. In addition to having a role in microbial infection, they have potential as biotechnological sensors and delivery systems. They share a similar monomeric architecture, with a variable membrane-binding domain and a structurally conserved pore-forming region. A significant portion of the monomeric subunit structure is re-organized to form the pore. Oligomers formed by members of the aerolysin family include: hepta- (aerolysin), octa- (Dln1), and nonameric oligomers (lysenin and monalysin).


Pssm-ID: 380802 [Multi-domain]  Cd Length: 151  Bit Score: 223.21  E-value: 5.55e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753936895 202 RPISISGSCISKSSVDQVYTVELKKTLSSSISRSWSDSTMNGIEVSETASMTVEGVAVSGTISTTISRQLENTFTVGEEE 281
Cdd:cd20232    1 EPIGISSSTQNGSDIEQVATLTLERELSKSTTRSFSESTLIGIEVSTTASVGVSAGPVSAEVEQTVTSTLENTFTIGKEE 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 753936895 282 ITSETAEYGQSVSITLPPNHRCEASIELTLKKYKVEANYIYRLKGSELKGKQKVTFEVDDYQAGEVKIETR 352
Cdd:cd20232   81 TKSETITFSKSVNVTIPPGNIGEAVMTLTPKKYKVEAIYTFRLKGTELKFKQKVIIEVDDYQTGEVKIEKF 151
XTALbg smart00247
Beta/gamma crystallins; Beta/gamma crystallins
 99-179 8.45e-09

Beta/gamma crystallins; Beta/gamma crystallins


Pssm-ID: 214583  Cd Length: 82  Bit Score: 51.74  E-value: 8.45e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753936895    99 VRFYEHANFTGfeQNLagteEVTE-YPS--PFLMNDSLTSLKVPEGCsVVLYKDTDFRGSSLELGAGE--HYLGHYGFND 173
Cdd:smart00247   2 ITLYEDENFQG--RSY----ELSDdCPSlqDYGSRDNVSSVRVESGC-WVLYEQPNYRGRQYVLEPGEypDYQEWGGFND 74


                   ....*.
gi 753936895   174 LVSSMK 179
Cdd:smart00247  75 QISSIR 80
XTALbg smart00247
Beta/gamma crystallins; Beta/gamma crystallins
 5-87 1.10e-07

Beta/gamma crystallins; Beta/gamma crystallins


Pssm-ID: 214583  Cd Length: 82  Bit Score: 48.66  E-value: 1.10e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753936895     5 LYKDANFNGTRRDFEEgEYPSIGD--IDNKVSSLKVGAGWYVeLYPGTGFRGDKVVLFTGEYgilpstISNGQISIWNDQ 82
Cdd:smart00247   4 LYEDENFQGRSYELSD-DCPSLQDygSRDNVSSVRVESGCWV-LYEQPNYRGRQYVLEPGEY------PDYQEWGGFNDQ 75


                   ....*
gi 753936895    83 ISSMK 87
Cdd:smart00247  76 ISSIR 80
Crystall pfam00030
Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity ...
 3-87 2.56e-05

Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity between them is very low.


Pssm-ID: 459639  Cd Length: 82  Bit Score: 42.10  E-value: 2.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753936895    3 VELYKDANFNGTRRDFEEgEYPSIGDID--NKVSSLKVGAG-WyvELYPGTGFRGDKVVLFTGEYgilPSTISNGQIsiw 79
Cdd:pfam00030   2 IVLYEKENFQGRSIELTD-DCPSLQERGfnSRVNSIRVLSGaW--VLYEHPNFRGRQYVLEPGEY---PDWSDWGAP--- 72


                  ....*...
gi 753936895   80 NDQISSMK 87
Cdd:pfam00030  73 NDRIGSLR 80
 
Name Accession Description Interval E-value
PFM_crystallin-like cd20232
pore-forming module (PFM) of uncharacterized proteins which have N-terminal crystallin domain ...
 202-352 5.55e-73

pore-forming module (PFM) of uncharacterized proteins which have N-terminal crystallin domain(s), and similar aerolysin-type beta-barrel pore-forming proteins; Many proteins belonging to this group have N-terminal crystallin (beta/gamma crystallins) domain(s). Members of this group belong to the aerolysin family of beta-pore-forming proteins (beta-PFPs). PFPs are generally secreted as water-soluble monomers, which upon binding to target lipid membranes, oligomerize and form transmembrane pores harmful to cells. Beta-PFPs form pores by transmembrane beta-barrels. Aerolysin-type beta-PFPs are believed to use an amphipathic beta-hairpin to form the beta-barrel, are found in all kingdoms of life and many are bacterial toxins. In addition to having a role in microbial infection, they have potential as biotechnological sensors and delivery systems. They share a similar monomeric architecture, with a variable membrane-binding domain and a structurally conserved pore-forming region. A significant portion of the monomeric subunit structure is re-organized to form the pore. Oligomers formed by members of the aerolysin family include: hepta- (aerolysin), octa- (Dln1), and nonameric oligomers (lysenin and monalysin).


Pssm-ID: 380802 [Multi-domain]  Cd Length: 151  Bit Score: 223.21  E-value: 5.55e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753936895 202 RPISISGSCISKSSVDQVYTVELKKTLSSSISRSWSDSTMNGIEVSETASMTVEGVAVSGTISTTISRQLENTFTVGEEE 281
Cdd:cd20232    1 EPIGISSSTQNGSDIEQVATLTLERELSKSTTRSFSESTLIGIEVSTTASVGVSAGPVSAEVEQTVTSTLENTFTIGKEE 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 753936895 282 ITSETAEYGQSVSITLPPNHRCEASIELTLKKYKVEANYIYRLKGSELKGKQKVTFEVDDYQAGEVKIETR 352
Cdd:cd20232   81 TKSETITFSKSVNVTIPPGNIGEAVMTLTPKKYKVEAIYTFRLKGTELKFKQKVIIEVDDYQTGEVKIEKF 151
XTALbg smart00247
Beta/gamma crystallins; Beta/gamma crystallins
 99-179 8.45e-09

Beta/gamma crystallins; Beta/gamma crystallins


Pssm-ID: 214583  Cd Length: 82  Bit Score: 51.74  E-value: 8.45e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753936895    99 VRFYEHANFTGfeQNLagteEVTE-YPS--PFLMNDSLTSLKVPEGCsVVLYKDTDFRGSSLELGAGE--HYLGHYGFND 173
Cdd:smart00247   2 ITLYEDENFQG--RSY----ELSDdCPSlqDYGSRDNVSSVRVESGC-WVLYEQPNYRGRQYVLEPGEypDYQEWGGFND 74


                   ....*.
gi 753936895   174 LVSSMK 179
Cdd:smart00247  75 QISSIR 80
XTALbg smart00247
Beta/gamma crystallins; Beta/gamma crystallins
 5-87 1.10e-07

Beta/gamma crystallins; Beta/gamma crystallins


Pssm-ID: 214583  Cd Length: 82  Bit Score: 48.66  E-value: 1.10e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753936895     5 LYKDANFNGTRRDFEEgEYPSIGD--IDNKVSSLKVGAGWYVeLYPGTGFRGDKVVLFTGEYgilpstISNGQISIWNDQ 82
Cdd:smart00247   4 LYEDENFQGRSYELSD-DCPSLQDygSRDNVSSVRVESGCWV-LYEQPNYRGRQYVLEPGEY------PDYQEWGGFNDQ 75


                   ....*
gi 753936895    83 ISSMK 87
Cdd:smart00247  76 ISSIR 80
Crystall pfam00030
Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity ...
 3-87 2.56e-05

Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity between them is very low.


Pssm-ID: 459639  Cd Length: 82  Bit Score: 42.10  E-value: 2.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753936895    3 VELYKDANFNGTRRDFEEgEYPSIGDID--NKVSSLKVGAG-WyvELYPGTGFRGDKVVLFTGEYgilPSTISNGQIsiw 79
Cdd:pfam00030   2 IVLYEKENFQGRSIELTD-DCPSLQERGfnSRVNSIRVLSGaW--VLYEHPNFRGRQYVLEPGEY---PDWSDWGAP--- 72


                  ....*...
gi 753936895   80 NDQISSMK 87
Cdd:pfam00030  73 NDRIGSLR 80
PFM_natterin-3-like cd20220
pore-forming module of Thalassophryne nattereri fish venom natterins 1-4, and similar ...
 257-317 3.56e-05

pore-forming module of Thalassophryne nattereri fish venom natterins 1-4, and similar aerolysin-type beta-barrel pore-forming proteins; This group includes 4 of the 5 Thalassophryne nattereri fish venom natterins: natterin-1, -2, -3, and 4. Natterins have kininogenase activity, kallikrein activity, and are allodynic and edema inducing. They also cleave type I and type IV collagen, resulting in necrosis of the affected cells. Contradictory to their edematic activity, Natterins also have anti-inflammatory effects through inhibition of interactions between leukocytes and the endothelium, and reduction in neutrophil accumulation. Many proteins belonging to this group have an N-terminal DUF3421 domain. They belong to the aerolysin family of beta-pore-forming proteins (beta-PFPs). PFPs are generally secreted as water-soluble monomers, which upon binding to target lipid membranes, oligomerize and form transmembrane pores harmful to cells. Beta-PFPs form pores by transmembrane beta-barrels. Aerolysin-type beta-PFPs are believed to use an amphipathic beta-hairpin to form the beta-barrel, are found in all kingdoms of life and many are bacterial toxins. In addition to having a role in microbial infection, they have potential as biotechnological sensors and delivery systems. They share a similar monomeric architecture, with a variable membrane-binding domain and a structurally conserved pore-forming region. A significant portion of the monomeric subunit structure is re-organized to form the pore. Oligomers formed by members of the aerolysin family include: hepta- (aerolysin), octa- (Dln1), and nonameric oligomers (lysenin and monalysin).


Pssm-ID: 380790 [Multi-domain]  Cd Length: 152  Bit Score: 43.38  E-value: 3.56e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 753936895 257 VAVSGTISTTI--------SRQLENTFTVGEEEITSETAEYGQSVSITLPPNHRCEasIELTLKKYKVE 317
Cdd:cd20220   46 LGVSTTITAGIpiiagggwEVSTETTFTWSGGTSVTESVTHSVSVEVTVPPNHSCT--VKMVGYKYKAD 112
PFM_aerolysin-like cd20240
pore-forming module of aerolysin-type beta-barrel pore-forming proteins; uncharacterized ...
 241-326 4.79e-05

pore-forming module of aerolysin-type beta-barrel pore-forming proteins; uncharacterized subgroup; Generally, pore-forming proteins (PFPs) are secreted as water-soluble monomers, which upon binding to target lipid membranes, oligomerize and form transmembrane pores detrimental to cells. Beta-PFPs form pores by transmembrane beta-barrels. Aerolysin-type beta-PFPs are believed to use an amphipathic beta-hairpin to form the beta-barrel. Many of this family are bacterial toxins. A significant portion of the monomeric subunit structure is re-organized to form the pore. Oligomers formed by members of the aerolysin family include: hepta- (aerolysin), octa- (Dln1), and nonameric oligomers (lysenin and monalysin).


Pssm-ID: 380810 [Multi-domain]  Cd Length: 145  Bit Score: 43.02  E-value: 4.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753936895 241 MNGIEVSETASMTV-EGVAVSGTISTTIsrQLENTFTVGEEEITSETAEYgqSVSITLPPNHRCEAsiELTLKKYKVEAN 319
Cdd:cd20240   40 TEGVSTTVSTSLKVgIPFIAGGEITTTT--TTSQSWTYGKSETKTDTISY--TFPIVVPPNTTVTA--TAVVTKYNMDVT 113


                 ....*..
gi 753936895 320 YIYRLKG 326
Cdd:cd20240  114 YVATLRG 120
PFM_LIN24-like cd20237
pore-forming module of Caenorhabditis elegans LIN-24 and similar aerolysin-type beta-barrel ...
 243-310 1.02e-04

pore-forming module of Caenorhabditis elegans LIN-24 and similar aerolysin-type beta-barrel pore-forming proteins; The process of cytotoxic cell death occurs in Caenorhabditis elegans containing mutations in either of lin-24 and lin-33. The cytotoxicity caused by mutation of either gene requires the function of the other. Genes required for the engulfment of apoptotic corpses function in the cytotoxic cell deaths induced by mutations in lin-24 and lin-33. It has been proposed that Caenorhabditis elegans LIN-24 may function to interact with bacterial toxins having similarity with it, and inactivate these, thereby allowing C. elegans to consume or survive exposure to bacteria that produce such toxins. Members of this group belong to the aerolysin family of beta-pore-forming proteins (beta-PFPs). PFPs are generally secreted as water-soluble monomers, which upon binding to target lipid membranes, oligomerize and form transmembrane pores harmful to cells. Beta-PFPs form pores by transmembrane beta-barrels. Aerolysin-type beta-PFPs are believed to use an amphipathic beta-hairpin to form the beta-barrel, are found in all kingdoms of life and many are bacterial toxins. In addition to having a role in microbial infection, they have potential as biotechnological sensors and delivery systems. They share a similar monomeric architecture, with a variable membrane-binding domain and a structurally conserved pore-forming region. A significant portion of the monomeric subunit structure is re-organized to form the pore. Oligomers formed by members of the aerolysin family include: hepta- (aerolysin), octa- (Dln1), and nonameric oligomers (lysenin and monalysin).


Pssm-ID: 380807  Cd Length: 120  Bit Score: 41.41  E-value: 1.02e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 753936895 243 GIEVSETASMTVEGVAVSGTISTTISRQLenTFTVGEEEITSETAEYGQSVSITLPPNHRCEASIELT 310
Cdd:cd20237   39 GFTIGGEVSLKLGPPPDIAEANAGFSREL--SLSKTQEETFEEELTWSVDSQVTVPPKTKVTAELVIT 104
PFM_aerolysin_family cd10140
pore-forming module of aerolysin-type beta-barrel pore-forming proteins; Pore-forming proteins ...
 264-339 3.57e-03

pore-forming module of aerolysin-type beta-barrel pore-forming proteins; Pore-forming proteins (PFPs) are generally secreted as water-soluble monomers, which upon binding to target lipid membranes, oligomerize and form transmembrane pores harmful to cells. Beta pore-forming proteins (beta-PFPs) form pores by transmembrane beta-barrels. Aerolysin-type beta-PFPs are believed to use an amphipathic beta-hairpin to form the beta-barrel, are found in all kingdoms of life and many are bacterial toxins. In addition to having a role in microbial infection, they have potential as biotechnological sensors and delivery systems. They share a similar monomeric architecture, with a variable membrane-binding domain and a structurally conserved pore-forming region. A significant portion of the monomeric subunit structure is re-organized to form the pore. Oligomers formed by members of the aerolysin family include: hepta- (aerolysin), octa- (Dln1), and nonameric oligomers (lysenin and monalysin). Members of this family includes enterolobin, a cytolytic, inflammatory and insecticidal protein from the Brazilian tree Enterolobium contortisiliquum.


Pssm-ID: 380782  Cd Length: 92  Bit Score: 36.37  E-value: 3.57e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 753936895 264 STTISRQLENT--FTVGEEEITSETAEYGQSVSITLPPNHRCEASIelTLKKYKVEANYIYRLKGSELKGKQKVTFEV 339
Cdd:cd10140    2 VVVGSQTVTNTssTTQTQTVTLSETKTVSVTVTVTVPPGKTVKVTV--TVTKAKIDVPYTATLKATYSTSGTGTTGTV 77
 
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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