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Conserved domains on  [gi|1039817338|ref|WP_064976917|]
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porin [Alistipes provencensis]

Protein Classification

porin family protein( domain architecture ID 229388)

porin family protein is a member of a large superfamily consisting of classical (gram-negative ) porins which are non-specific channels for small hydrophillic molecules, maltoporin-like channels which have specificities for various sugars, and ligand-gated protein channels which cooperate with a TonB associated inner membrane complex to actively transport ligands via the proton motive force

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
OM_channels super family cl21487
Porin superfamily. These outer membrane channels share a beta-barrel structure that differ in ...
81-415 1.20e-06

Porin superfamily. These outer membrane channels share a beta-barrel structure that differ in strand and shear number. Classical (gram-negative ) porins are non-specific channels for small hydrophillic molecules and form 16 beta-stranded barrels (16,20), which associate as trimers. Maltoporin-like channels have specificities for various sugars and form 18 beta-stranded barrels (18,22), which associate as trimers. Ligand-gated protein channels cooperate with a TonB associated inner membrane complex to actively transport ligands via the proton motive force and they form monomeric, (22,24) barrels. The 150-200 N-terminal residues form a plug that blocks the channel from the periplasmic end.


The actual alignment was detected with superfamily member pfam07396:

Pssm-ID: 473880  Cd Length: 371  Bit Score: 50.14  E-value: 1.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039817338  81 LSFDDDFTLTKTDARVKRLRLRFDGYIYSpKLVYSVQLGFTGYDTE-VLPNGSMNIVRDAIVYYVPSAKWNIGFGQTKIK 159
Cdd:pfam07396  14 FDGDDRDNDDTADFKFRRARLEVTGKLNG-KFSYTLRQDFNGSAGGtSLGDNLSGSFDDAYVDYTLFDKFALTVGKFKQP 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039817338 160 ANRARINSSSALQFVDRsivnSEFNLDRDFGFFG-----EYNLDRkSGFDLSAkgSVTlgEGRNWGSSSNGGMAYTGRLE 234
Cdd:pfam07396  93 FGLEELTSSNPGLFMER----SDLADYVNADCFGrgvgvGWQLNR-NQEVLQA--GVY--SGGSNDRNGNSGDTYAVRAT 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039817338 235 LYPlgrFSAKGDLLE----------------GDFDFEERPRILIAGAYSYNHKASRLKGQrGAIMPDDATRnlgsYFADF 298
Cdd:pfam07396 164 FAP---LLAAGNVLHlgasavpldytdnwngTFIDGRIQLRLSLSARPEAGLTNNRLITT-GALANVDGGR----WGLEA 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039817338 299 ILKYRGFAFYTDYMGRTCDEPlfdgDRNAFVYSGQGLNIQASYLF--------------------RNKWEVALRNSTLFP 358
Cdd:pfam07396 236 AWMYGPLSLQAEYLRSAVTRT----GAGAQDYKYLGGYVQGGYRLtgesrgyklgtakikppnhpYGAWELAARYDSLDL 311
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039817338 359 EEKvqPLAGYRNWNqTTLGVTRYIIGHsLKVQADMSYNTRSRSA-----DPNYNRWEIRFQL 415
Cdd:pfam07396 312 NDK--NVTGGRQDG-WTLGVNWYPKDN-LRFMLNYIKVKYDDETtarslDADTDALSLRLQY 369
 
Name Accession Description Interval E-value
Porin_O_P pfam07396
Phosphate-selective porin O and P; This family represents a conserved region approximately 400 ...
81-415 1.20e-06

Phosphate-selective porin O and P; This family represents a conserved region approximately 400 residues long within the bacterial phosphate-selective porins O and P. These are anion-specific porins, the binding site of which has a higher affinity for phosphate than chloride ions. Porin O has a higher affinity for polyphosphates, while porin P has a higher affinity for orthophosphate. In P. aeruginosa, porin O was found to be expressed only under phosphate-starvation conditions during the stationary growth phase.


Pssm-ID: 429442  Cd Length: 371  Bit Score: 50.14  E-value: 1.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039817338  81 LSFDDDFTLTKTDARVKRLRLRFDGYIYSpKLVYSVQLGFTGYDTE-VLPNGSMNIVRDAIVYYVPSAKWNIGFGQTKIK 159
Cdd:pfam07396  14 FDGDDRDNDDTADFKFRRARLEVTGKLNG-KFSYTLRQDFNGSAGGtSLGDNLSGSFDDAYVDYTLFDKFALTVGKFKQP 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039817338 160 ANRARINSSSALQFVDRsivnSEFNLDRDFGFFG-----EYNLDRkSGFDLSAkgSVTlgEGRNWGSSSNGGMAYTGRLE 234
Cdd:pfam07396  93 FGLEELTSSNPGLFMER----SDLADYVNADCFGrgvgvGWQLNR-NQEVLQA--GVY--SGGSNDRNGNSGDTYAVRAT 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039817338 235 LYPlgrFSAKGDLLE----------------GDFDFEERPRILIAGAYSYNHKASRLKGQrGAIMPDDATRnlgsYFADF 298
Cdd:pfam07396 164 FAP---LLAAGNVLHlgasavpldytdnwngTFIDGRIQLRLSLSARPEAGLTNNRLITT-GALANVDGGR----WGLEA 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039817338 299 ILKYRGFAFYTDYMGRTCDEPlfdgDRNAFVYSGQGLNIQASYLF--------------------RNKWEVALRNSTLFP 358
Cdd:pfam07396 236 AWMYGPLSLQAEYLRSAVTRT----GAGAQDYKYLGGYVQGGYRLtgesrgyklgtakikppnhpYGAWELAARYDSLDL 311
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039817338 359 EEKvqPLAGYRNWNqTTLGVTRYIIGHsLKVQADMSYNTRSRSA-----DPNYNRWEIRFQL 415
Cdd:pfam07396 312 NDK--NVTGGRQDG-WTLGVNWYPKDN-LRFMLNYIKVKYDDETtarslDADTDALSLRLQY 369
 
Name Accession Description Interval E-value
Porin_O_P pfam07396
Phosphate-selective porin O and P; This family represents a conserved region approximately 400 ...
81-415 1.20e-06

Phosphate-selective porin O and P; This family represents a conserved region approximately 400 residues long within the bacterial phosphate-selective porins O and P. These are anion-specific porins, the binding site of which has a higher affinity for phosphate than chloride ions. Porin O has a higher affinity for polyphosphates, while porin P has a higher affinity for orthophosphate. In P. aeruginosa, porin O was found to be expressed only under phosphate-starvation conditions during the stationary growth phase.


Pssm-ID: 429442  Cd Length: 371  Bit Score: 50.14  E-value: 1.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039817338  81 LSFDDDFTLTKTDARVKRLRLRFDGYIYSpKLVYSVQLGFTGYDTE-VLPNGSMNIVRDAIVYYVPSAKWNIGFGQTKIK 159
Cdd:pfam07396  14 FDGDDRDNDDTADFKFRRARLEVTGKLNG-KFSYTLRQDFNGSAGGtSLGDNLSGSFDDAYVDYTLFDKFALTVGKFKQP 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039817338 160 ANRARINSSSALQFVDRsivnSEFNLDRDFGFFG-----EYNLDRkSGFDLSAkgSVTlgEGRNWGSSSNGGMAYTGRLE 234
Cdd:pfam07396  93 FGLEELTSSNPGLFMER----SDLADYVNADCFGrgvgvGWQLNR-NQEVLQA--GVY--SGGSNDRNGNSGDTYAVRAT 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039817338 235 LYPlgrFSAKGDLLE----------------GDFDFEERPRILIAGAYSYNHKASRLKGQrGAIMPDDATRnlgsYFADF 298
Cdd:pfam07396 164 FAP---LLAAGNVLHlgasavpldytdnwngTFIDGRIQLRLSLSARPEAGLTNNRLITT-GALANVDGGR----WGLEA 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039817338 299 ILKYRGFAFYTDYMGRTCDEPlfdgDRNAFVYSGQGLNIQASYLF--------------------RNKWEVALRNSTLFP 358
Cdd:pfam07396 236 AWMYGPLSLQAEYLRSAVTRT----GAGAQDYKYLGGYVQGGYRLtgesrgyklgtakikppnhpYGAWELAARYDSLDL 311
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039817338 359 EEKvqPLAGYRNWNqTTLGVTRYIIGHsLKVQADMSYNTRSRSA-----DPNYNRWEIRFQL 415
Cdd:pfam07396 312 NDK--NVTGGRQDG-WTLGVNWYPKDN-LRFMLNYIKVKYDDETtarslDADTDALSLRLQY 369
 
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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