NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|15226849|ref|NP_181032|]
View 

DnaJ/Hsp40 cysteine-rich domain superfamily protein [Arabidopsis thaliana]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PRK14298 super family cl32989
chaperone protein DnaJ; Provisional
 102-157 2.98e-08

chaperone protein DnaJ; Provisional


The actual alignment was detected with superfamily member PRK14298:

Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 52.16  E-value: 2.98e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15226849  102 CRNCQGSGA------VLCDMCGGTGKWKALNRKRAKDVYEFTECPNCYGRGKLV---CPVCLGTG 157
Cdd:PRK14298 144 CSTCSGTGAkpgtspKRCPTCGGTGQVTTTRSTPLGQFVTTTTCSTCHGRGQVIespCPVCSGTG 208
 
Name Accession Description Interval E-value
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
 102-157 2.98e-08

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 52.16  E-value: 2.98e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15226849  102 CRNCQGSGA------VLCDMCGGTGKWKALNRKRAKDVYEFTECPNCYGRGKLV---CPVCLGTG 157
Cdd:PRK14298 144 CSTCSGTGAkpgtspKRCPTCGGTGQVTTTRSTPLGQFVTTTTCSTCHGRGQVIespCPVCSGTG 208
DnaJ_zf cd10719
Zinc finger domain of DnaJ and HSP40; Central/middle or CxxCxGxG-motif containing domain of ...
 102-157 4.44e-05

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: 39.93  E-value: 4.44e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15226849 102 CRNCQGSGA------VLCDMCGGTGKWKALNRKRAKDVYEFTECPNCYGRGKLV---CPVCLGTG 157
Cdd:cd10719   1 CPTCNGSGAkpgtkpKTCPTCGGSGQVRQVQGTGFGFFQTQTTCPTCGGTGKIIkdpCPKCKGKG 65
DnaJ_CXXCXGXG pfam00684
DnaJ central domain; The central cysteine-rich (CR) domain of DnaJ proteins contains four ...
 102-157 6.38e-05

DnaJ central domain; The central cysteine-rich (CR) domain of DnaJ proteins contains four repeats of the motif CXXCXGXG where X is any amino acid. The isolated cysteine rich domain folds in zinc dependent fashion. Each set of two repeats binds one unit of zinc. Although this domain has been implicated in substrate binding, no evidence of specific interaction between the isolated DNAJ cysteine rich domain and various hydrophobic peptides has been found.


Pssm-ID: 459904 [Multi-domain]  Cd Length: 65  Bit Score: 39.46  E-value: 6.38e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15226849   102 CRNCQGSGA------VLCDMCGGTGKWKALNRKRAKDVYEFTECPNCYGRGKLV---CPVCLGTG 157
Cdd:pfam00684   1 CPTCNGSGAkpgtkpTTCPTCGGTGQVRRVQQTGPGFFQMQSTCPTCGGTGKIIkdpCKKCKGKG 65
 
Name Accession Description Interval E-value
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
 102-157 2.98e-08

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 52.16  E-value: 2.98e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15226849  102 CRNCQGSGA------VLCDMCGGTGKWKALNRKRAKDVYEFTECPNCYGRGKLV---CPVCLGTG 157
Cdd:PRK14298 144 CSTCSGTGAkpgtspKRCPTCGGTGQVTTTRSTPLGQFVTTTTCSTCHGRGQVIespCPVCSGTG 208
PRK14276 PRK14276
chaperone protein DnaJ; Provisional
 101-157 7.47e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 237653 [Multi-domain]  Cd Length: 380  Bit Score: 48.16  E-value: 7.47e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15226849  101 SCRNCQGSGA------VLCDMCGGTG-----KWKALNRKRAKdvyefTECPNCYGRGKLV---CPVCLGTG 157
Cdd:PRK14276 148 TCHTCNGSGAkpgtspVTCGKCHGSGvitvdTQTPLGMMRRQ-----VTCDVCHGTGKEIkepCQTCHGTG 213
PRK14278 PRK14278
chaperone protein DnaJ; Provisional
 102-157 9.40e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 237654 [Multi-domain]  Cd Length: 378  Bit Score: 47.74  E-value: 9.40e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15226849  102 CRNCQGSGA------VLCDMCGGTGKWKALNRKRAKDVYEFTECPNCYGRGKLV---CPVCLGTG 157
Cdd:PRK14278 142 CDRCHGKGTagdskpVTCDTCGGRGEVQTVQRSFLGQVMTSRPCPTCRGVGEVIpdpCHECAGDG 206
PRK14290 PRK14290
chaperone protein DnaJ; Provisional
 102-157 9.95e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 172778 [Multi-domain]  Cd Length: 365  Bit Score: 47.62  E-value: 9.95e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15226849  102 CRNCQGSGA-----VLCDMCGGTGKWKALNRKRAKDVYEFTECPNCYGRGKL---VCPVCLGTG 157
Cdd:PRK14290 152 CPDCSGTGAkngklITCPTCHGTGQQRIVRGQGFFRMVTVTTCRTCGGRGRIpeeKCPRCNGTG 215
PRK14286 PRK14286
chaperone protein DnaJ; Provisional
 101-158 1.59e-06

chaperone protein DnaJ; Provisional


Pssm-ID: 172774 [Multi-domain]  Cd Length: 372  Bit Score: 47.29  E-value: 1.59e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15226849  101 SCRNCQGSGA------VLCDMCGGTGKWKalnrkRAKDVYEF-TECPNCYGRGKLV---CPVCLGTGL 158
Cdd:PRK14286 152 SCVDCNGSGAskgsspTTCPDCGGSGQIR-----RTQGFFSVaTTCPTCRGKGTVIsnpCKTCGGQGL 214
PRK14293 PRK14293
molecular chaperone DnaJ;
101-157 1.91e-06

molecular chaperone DnaJ;


Pssm-ID: 237663 [Multi-domain]  Cd Length: 374  Bit Score: 46.91  E-value: 1.91e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15226849  101 SCRNCQGSGA------VLCDMCGGTGKWKALNRKRAKDVYEFTECPNCYGRGKLV---CPVCLGTG 157
Cdd:PRK14293 145 TCETCRGSGAkpgtgpTTCSTCGGAGQVRRATRTPFGSFTQVSECPTCNGTGQVIedpCDACGGQG 210
PLN03165 PLN03165
chaperone protein dnaJ-related; Provisional
 102-158 2.38e-06

chaperone protein dnaJ-related; Provisional


Pssm-ID: 178709 [Multi-domain]  Cd Length: 111  Bit Score: 44.42  E-value: 2.38e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 15226849  102 CRNCQGSGAVLCDMCGGTGkwkALNRKRAKDVYEFTECPNCYGRGKLVCPVCLGTGL 158
Cdd:PLN03165  44 CFPCSGTGAQVCRFCVGSG---NVTVELGGGEKEVSKCINCDGAGSLTCTTCQGSGI 97
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 101-157 2.67e-06

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 46.29  E-value: 2.67e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15226849  101 SCRNCQGSGA------VLCDMCGGTGkwkalnRKRAKDVYeFT---ECPNCYGRGKLV---CPVCLGTG 157
Cdd:PRK10767 144 TCDTCHGSGAkpgtspKTCPTCHGAG------QVRMQQGF-FTvqqTCPTCHGRGKIIkdpCKKCHGQG 205
PRK14295 PRK14295
molecular chaperone DnaJ;
100-157 6.27e-06

molecular chaperone DnaJ;


Pssm-ID: 237665 [Multi-domain]  Cd Length: 389  Bit Score: 45.61  E-value: 6.27e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15226849  100 GSCRNCQGSGAV------LCDMCGGTGKwkalnRKRAKDVYEFTE-CPNCYGRGKLV---CPVCLGTG 157
Cdd:PRK14295 167 APCPACSGTGAKngttprVCPTCSGTGQ-----VSRNSGGFSLSEpCPDCKGRGLIAddpCLVCKGSG 229
PRK14297 PRK14297
molecular chaperone DnaJ;
101-157 7.35e-06

molecular chaperone DnaJ;


Pssm-ID: 184611 [Multi-domain]  Cd Length: 380  Bit Score: 45.16  E-value: 7.35e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15226849  101 SCRNCQGSGA------VLCDMCGGTGKWKALNRKRAKDVYEFTECPNCYGRGKLV---CPVCLGTG 157
Cdd:PRK14297 150 NCETCNGTGAkpgtspKTCDKCGGTGQIRVQRNTPLGSFVSTTTCDKCGGSGKVIedpCNKCHGKG 215
PRK14280 PRK14280
molecular chaperone DnaJ;
101-157 3.49e-05

molecular chaperone DnaJ;


Pssm-ID: 237656 [Multi-domain]  Cd Length: 376  Bit Score: 43.17  E-value: 3.49e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15226849  101 SCRNCQGSGA------VLCDMCGGTGKWKA-----LNRKRAKDVyefteCPNCYGRGKLV---CPVCLGTG 157
Cdd:PRK14280 145 TCDTCHGSGAkpgtskETCSHCGGSGQVSVeqntpFGRVVNRQT-----CPHCNGTGQEIkekCPTCHGKG 210
DnaJ_zf cd10719
Zinc finger domain of DnaJ and HSP40; Central/middle or CxxCxGxG-motif containing domain of ...
 102-157 4.44e-05

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: 39.93  E-value: 4.44e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15226849 102 CRNCQGSGA------VLCDMCGGTGKWKALNRKRAKDVYEFTECPNCYGRGKLV---CPVCLGTG 157
Cdd:cd10719   1 CPTCNGSGAkpgtkpKTCPTCGGSGQVRQVQGTGFGFFQTQTTCPTCGGTGKIIkdpCPKCKGKG 65
PRK14289 PRK14289
molecular chaperone DnaJ;
102-158 4.88e-05

molecular chaperone DnaJ;


Pssm-ID: 237660 [Multi-domain]  Cd Length: 386  Bit Score: 42.90  E-value: 4.88e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15226849  102 CRNCQGSGA------VLCDMCGGTGKWKALNRKRAKDVYEFTECPNCYGRGKLV---CPVCLGTGL 158
Cdd:PRK14289 157 CSHCHGTGAegnngsETCPTCKGSGSVTRVQNTILGTMQTQSTCPTCNGEGKIIkkkCKKCGGEGI 222
DnaJ_CXXCXGXG pfam00684
DnaJ central domain; The central cysteine-rich (CR) domain of DnaJ proteins contains four ...
 102-157 6.38e-05

DnaJ central domain; The central cysteine-rich (CR) domain of DnaJ proteins contains four repeats of the motif CXXCXGXG where X is any amino acid. The isolated cysteine rich domain folds in zinc dependent fashion. Each set of two repeats binds one unit of zinc. Although this domain has been implicated in substrate binding, no evidence of specific interaction between the isolated DNAJ cysteine rich domain and various hydrophobic peptides has been found.


Pssm-ID: 459904 [Multi-domain]  Cd Length: 65  Bit Score: 39.46  E-value: 6.38e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15226849   102 CRNCQGSGA------VLCDMCGGTGKWKALNRKRAKDVYEFTECPNCYGRGKLV---CPVCLGTG 157
Cdd:pfam00684   1 CPTCNGSGAkpgtkpTTCPTCGGTGQVRRVQQTGPGFFQMQSTCPTCGGTGKIIkdpCKKCKGKG 65
PRK14294 PRK14294
chaperone protein DnaJ; Provisional
 102-157 8.15e-05

chaperone protein DnaJ; Provisional


Pssm-ID: 237664 [Multi-domain]  Cd Length: 366  Bit Score: 42.06  E-value: 8.15e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15226849  102 CRNCQGSGA------VLCDMCGGTGKWKalnrkRAKDVYEF-TECPNCYGRGKLV---CPVCLGTG 157
Cdd:PRK14294 147 CEECHGSGCepgtspTTCPQCGGSGQVT-----QSQGFFSIrTTCPRCRGMGKVIvspCKTCHGQG 207
PRK14279 PRK14279
molecular chaperone DnaJ;
102-157 1.35e-04

molecular chaperone DnaJ;


Pssm-ID: 237655 [Multi-domain]  Cd Length: 392  Bit Score: 41.64  E-value: 1.35e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15226849  102 CRNCQGSGA------VLCDMCGGTGkwkALNRKRAkdVYEFTE-CPNCYGRGKLV---CPVCLGTG 157
Cdd:PRK14279 176 CTTCHGSGArpgtspKVCPTCNGSG---VISRNQG--AFGFSEpCTDCRGTGSIIedpCEECKGTG 236
PRK14283 PRK14283
chaperone protein DnaJ; Provisional
 107-158 1.36e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 184604 [Multi-domain]  Cd Length: 378  Bit Score: 41.35  E-value: 1.36e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 15226849  107 GSGAVLCDMCGGTGKWKALNRKRAKDVYEFTECPNCYGRGKLV---CPVCLGTGL 158
Cdd:PRK14283 160 GSEVKTCPTCGGTGQVKQVRNTILGQMMNVTTCPDCQGEGKIVekpCSNCHGKGV 214
PRK14301 PRK14301
chaperone protein DnaJ; Provisional
 101-157 2.56e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 237668 [Multi-domain]  Cd Length: 373  Bit Score: 40.50  E-value: 2.56e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15226849  101 SCRNCQGSGAV------LCDMCGGTGKwkalnRKRAKDVYEF-TECPNCYGRGKLV---CPVCLGTG 157
Cdd:PRK14301 146 TCDDCGGSGAApgtspeTCRHCGGSGQ-----VRQSQGFFQIaVPCPVCRGEGRVIthpCPKCKGSG 207
PRK14285 PRK14285
chaperone protein DnaJ; Provisional
 102-157 7.64e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 172773 [Multi-domain]  Cd Length: 365  Bit Score: 39.20  E-value: 7.64e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15226849  102 CRNC------QGSGAVLCDMCGGTGKwkalnRKRAKDVYEFTE-CPNCYGRGKLV---CPVCLGTG 157
Cdd:PRK14285 149 CESClgkkseKGTSPSICNMCNGSGR-----VMQGGGFFRVTTtCPKCYGNGKIIsnpCKSCKGKG 209
PRK14282 PRK14282
chaperone protein DnaJ; Provisional
 102-157 1.20e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 184603 [Multi-domain]  Cd Length: 369  Bit Score: 38.62  E-value: 1.20e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15226849  102 CRNCQG------SGAVLCDMCGGTGKWKALNRK-RAKDVYEFTeCPNCYGRGKL---VCPVCLGTG 157
Cdd:PRK14282 155 CPHCGGtgvepgSGYVTCPKCHGTGRIREERRSfFGVFVSERT-CERCGGTGKIpgeYCHECGGSG 219
PRK14291 PRK14291
chaperone protein DnaJ; Provisional
 101-158 1.35e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 237661 [Multi-domain]  Cd Length: 382  Bit Score: 38.60  E-value: 1.35e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15226849  101 SCRNCQG------SGAVLCDMCGGTGKwkalNRKRAKDVYEFTECPNCYGRGKL--VCPVCLGTGL 158
Cdd:PRK14291 158 PCEACGGtgydpgSGEKVCPTCGGSGE----IYQRGGFFRISQTCPTCGGEGVLrePCSKCNGRGL 219
PRK14284 PRK14284
chaperone protein DnaJ; Provisional
 101-162 3.75e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 237658 [Multi-domain]  Cd Length: 391  Bit Score: 37.13  E-value: 3.75e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15226849  101 SCRNCQGSGAV------LCDMCGGTGKwkaLNRKRAKDVYEFTeCPNCYGRGKLV---CPVCLGTGLPNNK 162
Cdd:PRK14284 160 SCDACSGSGANssqgikVCDRCKGSGQ---VVQSRGFFSMAST-CPECGGEGRVItdpCSVCRGQGRIKDK 226
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH