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Conserved domains on  [gi|1002286729|ref|XP_015647661|]
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chaperonin-like RbcX protein 2, chloroplastic [Oryza sativa Japonica Group]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RbcX super family cl03549
RbcX protein; The RBCX protein has been identified as having a possible chaperone-like ...
 82-178 2.32e-16

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.


The actual alignment was detected with superfamily member pfam02341:

Pssm-ID: 426729  Cd Length: 100  Bit Score: 70.73  E-value: 2.32e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286729  82 IMNYFTYKATSTVLHQLYEMNPPAYTWLYNYVVVNDPKEGKHFLIALAKERQDLAERVMITRLHLYSK---WIKKCDHAk 158
Cdd:pfam02341   5 LQSYLTYQAVRTVLAQLSETNPPLAIWLSQFSSTHSLQDGEAYLEALMRENKELALRIMTVREHLAEEvleFLPEMVRT- 83

                          90       100
                  ....*....|....*....|
gi 1002286729 159 myeKISNENLEIMRQRLMET 178
Cdd:pfam02341  84 ---GIQQANMEHRRQLLERL 100
 
Name Accession Description Interval E-value
RbcX pfam02341
RbcX protein; The RBCX protein has been identified as having a possible chaperone-like ...
 82-178 2.32e-16

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: 70.73  E-value: 2.32e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286729  82 IMNYFTYKATSTVLHQLYEMNPPAYTWLYNYVVVNDPKEGKHFLIALAKERQDLAERVMITRLHLYSK---WIKKCDHAk 158
Cdd:pfam02341   5 LQSYLTYQAVRTVLAQLSETNPPLAIWLSQFSSTHSLQDGEAYLEALMRENKELALRIMTVREHLAEEvleFLPEMVRT- 83

                          90       100
                  ....*....|....*....|
gi 1002286729 159 myeKISNENLEIMRQRLMET 178
Cdd:pfam02341  84 ---GIQQANMEHRRQLLERL 100
 
Name Accession Description Interval E-value
RbcX pfam02341
RbcX protein; The RBCX protein has been identified as having a possible chaperone-like ...
 82-178 2.32e-16

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: 70.73  E-value: 2.32e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286729  82 IMNYFTYKATSTVLHQLYEMNPPAYTWLYNYVVVNDPKEGKHFLIALAKERQDLAERVMITRLHLYSK---WIKKCDHAk 158
Cdd:pfam02341   5 LQSYLTYQAVRTVLAQLSETNPPLAIWLSQFSSTHSLQDGEAYLEALMRENKELALRIMTVREHLAEEvleFLPEMVRT- 83

                          90       100
                  ....*....|....*....|
gi 1002286729 159 myeKISNENLEIMRQRLMET 178
Cdd:pfam02341  84 ---GIQQANMEHRRQLLERL 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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