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Conserved domains on  [gi|495030303|ref|WP_007755858|]
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MULTISPECIES: rod shape-determining protein MreD [Bacteroides]

Protein Classification

rod shape-determining protein MreD( domain architecture ID 10022433)

rod shape-determining protein MreD is involved in formation of the rod shape of the cell; may also contribute to regulation of formation of penicillin-binding proteins

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
shape_MreD TIGR03426
rod shape-determining protein MreD; Members of this protein family are the MreD protein of ...
 8-140 2.66e-09

rod shape-determining protein MreD; Members of this protein family are the MreD protein of bacterial cell shape determination. Most rod-shaped bacteria depend on MreB and RodA to achieve either a rod shape or some other non-spherical morphology such as coil or stalk formation. MreD is encoded in an operon with MreB, and often with RodA and PBP-2 as well. It is highly hydrophobic (therefore somewhat low-complexity) and highly divergent, and therefore sometimes tricky to discover by homology, but this model finds most examples. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]


:

Pssm-ID: 274574  Cd Length: 152  Bit Score: 52.99  E-value: 2.66e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495030303    8 RIGWFIGLVLLQVLILNNVHIAG----YATPFLYIYFILKFDSGTSRNELMLWAFFFGLTIDVFADTP-GMNAAATVLLA 82
Cdd:TIGR03426   1 LPIILILLSLLLALLLQLIPLPGffldGFRPDWVLLVLLYWAIALPHRVGIGTAFVLGLLQDVLSGSPlGVHALALTLVA 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 495030303   83 FLRPSLLRLFTPRDNLDSFIPSFKTIGITPFLKYTTASVFvhSLALLSIEFFSFSSIW 140
Cdd:TIGR03426  81 YLAASLFQRFRQFDLWQQALIIFLLLILGELLVFLILTLL--GNAFFSLEYFWLFRLL 136
 
Name Accession Description Interval E-value
shape_MreD TIGR03426
rod shape-determining protein MreD; Members of this protein family are the MreD protein of ...
 8-140 2.66e-09

rod shape-determining protein MreD; Members of this protein family are the MreD protein of bacterial cell shape determination. Most rod-shaped bacteria depend on MreB and RodA to achieve either a rod shape or some other non-spherical morphology such as coil or stalk formation. MreD is encoded in an operon with MreB, and often with RodA and PBP-2 as well. It is highly hydrophobic (therefore somewhat low-complexity) and highly divergent, and therefore sometimes tricky to discover by homology, but this model finds most examples. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]


Pssm-ID: 274574  Cd Length: 152  Bit Score: 52.99  E-value: 2.66e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495030303    8 RIGWFIGLVLLQVLILNNVHIAG----YATPFLYIYFILKFDSGTSRNELMLWAFFFGLTIDVFADTP-GMNAAATVLLA 82
Cdd:TIGR03426   1 LPIILILLSLLLALLLQLIPLPGffldGFRPDWVLLVLLYWAIALPHRVGIGTAFVLGLLQDVLSGSPlGVHALALTLVA 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 495030303   83 FLRPSLLRLFTPRDNLDSFIPSFKTIGITPFLKYTTASVFvhSLALLSIEFFSFSSIW 140
Cdd:TIGR03426  81 YLAASLFQRFRQFDLWQQALIIFLLLILGELLVFLILTLL--GNAFFSLEYFWLFRLL 136
 
Name Accession Description Interval E-value
shape_MreD TIGR03426
rod shape-determining protein MreD; Members of this protein family are the MreD protein of ...
 8-140 2.66e-09

rod shape-determining protein MreD; Members of this protein family are the MreD protein of bacterial cell shape determination. Most rod-shaped bacteria depend on MreB and RodA to achieve either a rod shape or some other non-spherical morphology such as coil or stalk formation. MreD is encoded in an operon with MreB, and often with RodA and PBP-2 as well. It is highly hydrophobic (therefore somewhat low-complexity) and highly divergent, and therefore sometimes tricky to discover by homology, but this model finds most examples. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]


Pssm-ID: 274574  Cd Length: 152  Bit Score: 52.99  E-value: 2.66e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495030303    8 RIGWFIGLVLLQVLILNNVHIAG----YATPFLYIYFILKFDSGTSRNELMLWAFFFGLTIDVFADTP-GMNAAATVLLA 82
Cdd:TIGR03426   1 LPIILILLSLLLALLLQLIPLPGffldGFRPDWVLLVLLYWAIALPHRVGIGTAFVLGLLQDVLSGSPlGVHALALTLVA 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 495030303   83 FLRPSLLRLFTPRDNLDSFIPSFKTIGITPFLKYTTASVFvhSLALLSIEFFSFSSIW 140
Cdd:TIGR03426  81 YLAASLFQRFRQFDLWQQALIIFLLLILGELLVFLILTLL--GNAFFSLEYFWLFRLL 136
 
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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