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Conserved domains on  [gi|1002274681|ref|XP_015641657|]
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protein BUNDLE SHEATH DEFECTIVE 2, chloroplastic [Oryza sativa Japonica Group]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK14294 super family cl36362
chaperone protein DnaJ; Provisional
 61-117 5.49e-05

chaperone protein DnaJ; Provisional


The actual alignment was detected with superfamily member PRK14294:

Pssm-ID: 237664 [Multi-domain]  Cd Length: 366  Bit Score: 41.29  E-value: 5.49e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002274681  61 SLVCQDCEGNGA------IVCNQCKGDGvnSVDHFNGRFKAGALCWLCRGKREIL---CGSCNGAG 117
Cdd:PRK14294  144 LETCEECHGSGCepgtspTTCPQCGGSG--QVTQSQGFFSIRTTCPRCRGMGKVIvspCKTCHGQG 207
 
Name Accession Description Interval E-value
PRK14294 PRK14294
chaperone protein DnaJ; Provisional
 61-117 5.49e-05

chaperone protein DnaJ; Provisional


Pssm-ID: 237664 [Multi-domain]  Cd Length: 366  Bit Score: 41.29  E-value: 5.49e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002274681  61 SLVCQDCEGNGA------IVCNQCKGDGvnSVDHFNGRFKAGALCWLCRGKREIL---CGSCNGAG 117
Cdd:PRK14294  144 LETCEECHGSGCepgtspTTCPQCGGSG--QVTQSQGFFSIRTTCPRCRGMGKVIvspCKTCHGQG 207
DnaJ_zf cd10719
Zinc finger domain of DnaJ and HSP40; Central/middle or CxxCxGxG-motif containing domain of ...
 64-117 1.02e-03

Zinc finger domain of DnaJ and HSP40; Central/middle or CxxCxGxG-motif containing domain of DnaJ/Hsp40 (heat shock protein 40). DnaJ proteins are highly conserved and play crucial roles in protein translation, folding, unfolding, translocation, and degradation. They act primarily by stimulating the ATPase activity of Hsp70s, an important chaperonin family. Hsp40 proteins are characterized by the presence of an N-terminal J domain, which mediates the interaction with Hsp70. This central domain contains four repeats of a CxxCxGxG motif and binds to two Zinc ions. It has been implicated in substrate binding.


Pssm-ID: 199908 [Multi-domain]  Cd Length: 65  Bit Score: 35.31  E-value: 1.02e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002274681  64 CQDCEGNGA------IVCNQCKGDG--VNSVDHFNGRFKAGALCWLCRGKREIL---CGSCNGAG 117
Cdd:cd10719     1 CPTCNGSGAkpgtkpKTCPTCGGSGqvRQVQGTGFGFFQTQTTCPTCGGTGKIIkdpCPKCKGKG 65
 
Name Accession Description Interval E-value
PRK14294 PRK14294
chaperone protein DnaJ; Provisional
 61-117 5.49e-05

chaperone protein DnaJ; Provisional


Pssm-ID: 237664 [Multi-domain]  Cd Length: 366  Bit Score: 41.29  E-value: 5.49e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002274681  61 SLVCQDCEGNGA------IVCNQCKGDGvnSVDHFNGRFKAGALCWLCRGKREIL---CGSCNGAG 117
Cdd:PRK14294  144 LETCEECHGSGCepgtspTTCPQCGGSG--QVTQSQGFFSIRTTCPRCRGMGKVIvspCKTCHGQG 207
PRK14290 PRK14290
chaperone protein DnaJ; Provisional
 52-117 3.15e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 172778 [Multi-domain]  Cd Length: 365  Bit Score: 39.14  E-value: 3.15e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002274681  52 TEKSPPKGSSLVCQDCEGNGA-----IVCNQCKGDGVNSVDHFNGRFKAGAL--CWLCRGKREI---LCGSCNGAG 117
Cdd:PRK14290  140 TEKRIKYRRNAMCPDCSGTGAkngklITCPTCHGTGQQRIVRGQGFFRMVTVttCRTCGGRGRIpeeKCPRCNGTG 215
PRK14285 PRK14285
chaperone protein DnaJ; Provisional
 61-119 9.73e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 172773 [Multi-domain]  Cd Length: 365  Bit Score: 37.66  E-value: 9.73e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002274681  61 SLVCQDC------EGNGAIVCNQCKGDGvnSVDHFNGRFKAGALCWLCRGKREIL---CGSCNGAGFL 119
Cdd:PRK14285  146 NMLCESClgkkseKGTSPSICNMCNGSG--RVMQGGGFFRVTTTCPKCYGNGKIIsnpCKSCKGKGSL 211
DnaJ_zf cd10719
Zinc finger domain of DnaJ and HSP40; Central/middle or CxxCxGxG-motif containing domain of ...
 64-117 1.02e-03

Zinc finger domain of DnaJ and HSP40; Central/middle or CxxCxGxG-motif containing domain of DnaJ/Hsp40 (heat shock protein 40). DnaJ proteins are highly conserved and play crucial roles in protein translation, folding, unfolding, translocation, and degradation. They act primarily by stimulating the ATPase activity of Hsp70s, an important chaperonin family. Hsp40 proteins are characterized by the presence of an N-terminal J domain, which mediates the interaction with Hsp70. This central domain contains four repeats of a CxxCxGxG motif and binds to two Zinc ions. It has been implicated in substrate binding.


Pssm-ID: 199908 [Multi-domain]  Cd Length: 65  Bit Score: 35.31  E-value: 1.02e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002274681  64 CQDCEGNGA------IVCNQCKGDG--VNSVDHFNGRFKAGALCWLCRGKREIL---CGSCNGAG 117
Cdd:cd10719     1 CPTCNGSGAkpgtkpKTCPTCGGSGqvRQVQGTGFGFFQTQTTCPTCGGTGKIIkdpCPKCKGKG 65
PRK14286 PRK14286
chaperone protein DnaJ; Provisional
 50-118 1.55e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 172774 [Multi-domain]  Cd Length: 372  Bit Score: 36.89  E-value: 1.55e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002274681  50 DQTEKSPPKGSS-LVCQDCEGNGAIVCNQckgdgvnsvdhfnGRFKAGALCWLCRGKREIL---CGSCNGAGF 118
Cdd:PRK14286  155 DCNGSGASKGSSpTTCPDCGGSGQIRRTQ-------------GFFSVATTCPTCRGKGTVIsnpCKTCGGQGL 214
 
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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