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Conserved domains on  [gi|340780599|pdb|3RG6|E]
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Chain E, RbcX protein

Protein Classification

chaperonin family protein RbcX( domain architecture ID 10492219)

chaperonin family protein RbcX is an assembly chaperone for hexadecameric Rubisco

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RbcX pfam02341
RbcX protein; The RBCX protein has been identified as having a possible chaperone-like ...
 30-128 2.78e-62

RbcX protein; The RBCX protein has been identified as having a possible chaperone-like function. The rbcX gene is juxtaposed to and cotranscribed with rbcL and rbcS encoding RuBisCO in Anabaena sp. CA. RbcX has been shown to possess a chaperone-like function assisting correct folding of RuBisCO in E. coli expression studies and is needed for RuBisCO to reach its maximal activity.


:

Pssm-ID: 426729  Cd Length: 100  Bit Score: 186.67  E-value: 2.78e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3RG6_E         30 TAKTLQSYLTYQALRTVLAQLGETNPPLALWLHNFSA-GKVQDGEKYIEELFLEKPDLALRIMTVREHIAEEIAEFLPEM 108
Cdd:pfam02341   1 TAKVLQSYLTYQAVRTVLAQLSETNPPLAIWLSQFSStHSLQDGEAYLEALMRENKELALRIMTVREHLAEEVLEFLPEM 80

                          90       100
                  ....*....|....*....|
3RG6_E        109 VVTGIQQANMEKRRQHLERM 128
Cdd:pfam02341  81 VRTGIQQANMEHRRQLLERL 100
 
Name Accession Description Interval E-value
RbcX pfam02341
RbcX protein; The RBCX protein has been identified as having a possible chaperone-like ...
 30-128 2.78e-62

RbcX protein; The RBCX protein has been identified as having a possible chaperone-like function. The rbcX gene is juxtaposed to and cotranscribed with rbcL and rbcS encoding RuBisCO in Anabaena sp. CA. RbcX has been shown to possess a chaperone-like function assisting correct folding of RuBisCO in E. coli expression studies and is needed for RuBisCO to reach its maximal activity.


Pssm-ID: 426729  Cd Length: 100  Bit Score: 186.67  E-value: 2.78e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3RG6_E         30 TAKTLQSYLTYQALRTVLAQLGETNPPLALWLHNFSA-GKVQDGEKYIEELFLEKPDLALRIMTVREHIAEEIAEFLPEM 108
Cdd:pfam02341   1 TAKVLQSYLTYQAVRTVLAQLSETNPPLAIWLSQFSStHSLQDGEAYLEALMRENKELALRIMTVREHLAEEVLEFLPEM 80

                          90       100
                  ....*....|....*....|
3RG6_E        109 VVTGIQQANMEKRRQHLERM 128
Cdd:pfam02341  81 VRTGIQQANMEHRRQLLERL 100
 
Name Accession Description Interval E-value
RbcX pfam02341
RbcX protein; The RBCX protein has been identified as having a possible chaperone-like ...
 30-128 2.78e-62

RbcX protein; The RBCX protein has been identified as having a possible chaperone-like function. The rbcX gene is juxtaposed to and cotranscribed with rbcL and rbcS encoding RuBisCO in Anabaena sp. CA. RbcX has been shown to possess a chaperone-like function assisting correct folding of RuBisCO in E. coli expression studies and is needed for RuBisCO to reach its maximal activity.


Pssm-ID: 426729  Cd Length: 100  Bit Score: 186.67  E-value: 2.78e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3RG6_E         30 TAKTLQSYLTYQALRTVLAQLGETNPPLALWLHNFSA-GKVQDGEKYIEELFLEKPDLALRIMTVREHIAEEIAEFLPEM 108
Cdd:pfam02341   1 TAKVLQSYLTYQAVRTVLAQLSETNPPLAIWLSQFSStHSLQDGEAYLEALMRENKELALRIMTVREHLAEEVLEFLPEM 80

                          90       100
                  ....*....|....*....|
3RG6_E        109 VVTGIQQANMEKRRQHLERM 128
Cdd:pfam02341  81 VRTGIQQANMEHRRQLLERL 100
 
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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