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Conserved domains on  [gi|330254382|gb|AEC09476|]
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chaperone protein dnaJ-like protein [Arabidopsis thaliana]

Protein Classification

J domain-containing protein( domain architecture ID 1000550)

J domain-containing protein similar to molecular chaperone DnaJ, a protein that plays crucial roles in protein translation, folding, unfolding, translocation, and degradation, primarily by stimulating the ATPase activity of Hsp70

CATH:  1.10.287.110
Gene Ontology:  GO:0006457
PubMed:  35729039|9644977|8016869|15170475
SCOP:  4000605

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK14298 super family cl32989
chaperone protein DnaJ; Provisional
 153-272 6.94e-07

chaperone protein DnaJ; Provisional


The actual alignment was detected with superfamily member PRK14298:

Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 51.00  E-value: 6.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254382 153 FTGGEFNGKKHGSEPGLwelDLRPQfptLFVPYKE------TQVLVPNSEtveKCTGCTGRGdvvcptcnadGEPGfyke 226
Cdd:PRK14298  99 FFGGGGRRGRMGPRRGS---DLRYD---LYITLEEaafgvrKDIDVPRAE---RCSTCSGTG----------AKPG---- 155

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 330254382 227 NQMMKCSTCYGRGLVAHKDG-------SDTICTNCNGKGKL---PCPTCQSRGLIK 272
Cdd:PRK14298 156 TSPKRCPTCGGTGQVTTTRStplgqfvTTTTCSTCHGRGQViesPCPVCSGTGKVR 211
 
Name Accession Description Interval E-value
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
 153-272 6.94e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 51.00  E-value: 6.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254382 153 FTGGEFNGKKHGSEPGLwelDLRPQfptLFVPYKE------TQVLVPNSEtveKCTGCTGRGdvvcptcnadGEPGfyke 226
Cdd:PRK14298  99 FFGGGGRRGRMGPRRGS---DLRYD---LYITLEEaafgvrKDIDVPRAE---RCSTCSGTG----------AKPG---- 155

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 330254382 227 NQMMKCSTCYGRGLVAHKDG-------SDTICTNCNGKGKL---PCPTCQSRGLIK 272
Cdd:PRK14298 156 TSPKRCPTCGGTGQVTTTRStplgqfvTTTTCSTCHGRGQViesPCPVCSGTGKVR 211
DnaJ_zf cd10719
Zinc finger domain of DnaJ and HSP40; Central/middle or CxxCxGxG-motif containing domain of ...
 212-269 3.84e-06

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: 44.17  E-value: 3.84e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 330254382 212 CPTCNADG-EPGfykeNQMMKCSTCYGRGLVAHKDGSD-------TICTNCNGKGKL---PCPTCQSRG 269
Cdd:cd10719    1 CPTCNGSGaKPG----TKPKTCPTCGGSGQVRQVQGTGfgffqtqTTCPTCGGTGKIikdPCPKCKGKG 65
DnaJ_CXXCXGXG pfam00684
DnaJ central domain; The central cysteine-rich (CR) domain of DnaJ proteins contains four ...
 232-280 2.98e-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: 41.78  E-value: 2.98e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 330254382  232 CSTCYGRGlvAHKDGSDTICTNCNGKGKL---------------PCPTCQSRGLI---KCQTCDSTG 280
Cdd:pfam00684   1 CPTCNGSG--AKPGTKPTTCPTCGGTGQVrrvqqtgpgffqmqsTCPTCGGTGKIikdPCKKCKGKG 65
 
Name Accession Description Interval E-value
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
 153-272 6.94e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 51.00  E-value: 6.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254382 153 FTGGEFNGKKHGSEPGLwelDLRPQfptLFVPYKE------TQVLVPNSEtveKCTGCTGRGdvvcptcnadGEPGfyke 226
Cdd:PRK14298  99 FFGGGGRRGRMGPRRGS---DLRYD---LYITLEEaafgvrKDIDVPRAE---RCSTCSGTG----------AKPG---- 155

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 330254382 227 NQMMKCSTCYGRGLVAHKDG-------SDTICTNCNGKGKL---PCPTCQSRGLIK 272
Cdd:PRK14298 156 TSPKRCPTCGGTGQVTTTRStplgqfvTTTTCSTCHGRGQViesPCPVCSGTGKVR 211
DnaJ_zf cd10719
Zinc finger domain of DnaJ and HSP40; Central/middle or CxxCxGxG-motif containing domain of ...
 212-269 3.84e-06

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: 44.17  E-value: 3.84e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 330254382 212 CPTCNADG-EPGfykeNQMMKCSTCYGRGLVAHKDGSD-------TICTNCNGKGKL---PCPTCQSRG 269
Cdd:cd10719    1 CPTCNGSGaKPG----TKPKTCPTCGGSGQVRQVQGTGfgffqtqTTCPTCGGTGKIikdPCPKCKGKG 65
PRK14290 PRK14290
chaperone protein DnaJ; Provisional
 201-258 5.02e-06

chaperone protein DnaJ; Provisional


Pssm-ID: 172778 [Multi-domain]  Cd Length: 365  Bit Score: 48.39  E-value: 5.02e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 330254382 201 CTGCTGRGD-----VVCPTCNADGEP------GFYKENQMMKCSTCYGRGLVAHKDgsdtiCTNCNGKG 258
Cdd:PRK14290 152 CPDCSGTGAkngklITCPTCHGTGQQrivrgqGFFRMVTVTTCRTCGGRGRIPEEK-----CPRCNGTG 215
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 231-296 6.73e-06

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 47.83  E-value: 6.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254382 231 KCSTCYGRGlvaHKDGSDTI-CTNCNGKGKL-----------PCPTCQSRGLI---KCQTCDSTGSlltssiaVVKWKTL 295
Cdd:PRK10767 144 TCDTCHGSG---AKPGTSPKtCPTCHGAGQVrmqqgfftvqqTCPTCHGRGKIikdPCKKCHGQGR-------VEKEKTL 213


                 .
gi 330254382 296 S 296
Cdd:PRK10767 214 S 214
PRK14294 PRK14294
chaperone protein DnaJ; Provisional
 211-269 2.02e-05

chaperone protein DnaJ; Provisional


Pssm-ID: 237664 [Multi-domain]  Cd Length: 366  Bit Score: 46.30  E-value: 2.02e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 330254382 211 VCPTCNADG-EPGfykeNQMMKCSTCYGRGLVAHKDGSDTI---CTNCNGKGKL---PCPTCQSRG 269
Cdd:PRK14294 146 TCEECHGSGcEPG----TSPTTCPQCGGSGQVTQSQGFFSIrttCPRCRGMGKVivsPCKTCHGQG 207
PRK14291 PRK14291
chaperone protein DnaJ; Provisional
 210-271 2.94e-05

chaperone protein DnaJ; Provisional


Pssm-ID: 237661 [Multi-domain]  Cd Length: 382  Bit Score: 45.92  E-value: 2.94e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 330254382 210 VVCPTCNADGepgfYKENQMMK-CSTCYGRGLVAHKDGSDTI---CTNCNGKGKL--PCPTCQSRGLI 271
Cdd:PRK14291 157 VPCEACGGTG----YDPGSGEKvCPTCGGSGEIYQRGGFFRIsqtCPTCGGEGVLrePCSKCNGRGLV 220
DnaJ_CXXCXGXG pfam00684
DnaJ central domain; The central cysteine-rich (CR) domain of DnaJ proteins contains four ...
 232-280 2.98e-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: 41.78  E-value: 2.98e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 330254382  232 CSTCYGRGlvAHKDGSDTICTNCNGKGKL---------------PCPTCQSRGLI---KCQTCDSTG 280
Cdd:pfam00684   1 CPTCNGSG--AKPGTKPTTCPTCGGTGQVrrvqqtgpgffqmqsTCPTCGGTGKIikdPCKKCKGKG 65
PRK14290 PRK14290
chaperone protein DnaJ; Provisional
 207-271 4.27e-05

chaperone protein DnaJ; Provisional


Pssm-ID: 172778 [Multi-domain]  Cd Length: 365  Bit Score: 45.31  E-value: 4.27e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 330254382 207 RGDVVCPTCNADGEpgfyKENQMMKCSTCYGRGL--VAHKDG-----SDTICTNCNGKGKLP---CPTCQSRGLI 271
Cdd:PRK14290 147 RRNAMCPDCSGTGA----KNGKLITCPTCHGTGQqrIVRGQGffrmvTVTTCRTCGGRGRIPeekCPRCNGTGTV 217
PRK14283 PRK14283
chaperone protein DnaJ; Provisional
 187-258 6.60e-05

chaperone protein DnaJ; Provisional


Pssm-ID: 184604 [Multi-domain]  Cd Length: 378  Bit Score: 44.82  E-value: 6.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254382 187 ETQVLVPNSETVEKCTGCT---GRGDVVCPTCNADGEPGFYKEN---QMM---KCSTCYGRGLVAHKDgsdtiCTNCNGK 257
Cdd:PRK14283 138 EKDIKVRHTKKCPVCNGSRaepGSEVKTCPTCGGTGQVKQVRNTilgQMMnvtTCPDCQGEGKIVEKP-----CSNCHGK 212


                 .
gi 330254382 258 G 258
Cdd:PRK14283 213 G 213
DnaJ_CXXCXGXG pfam00684
DnaJ central domain; The central cysteine-rich (CR) domain of DnaJ proteins contains four ...
 212-269 2.02e-04

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: 39.08  E-value: 2.02e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 330254382  212 CPTCNADG-EPGfykeNQMMKCSTCYGRGLVAHKDGSD-------TICTNCNGKGKL---PCPTCQSRG 269
Cdd:pfam00684   1 CPTCNGSGaKPG----TKPTTCPTCGGTGQVRRVQQTGpgffqmqSTCPTCGGTGKIikdPCKKCKGKG 65
PRK14276 PRK14276
chaperone protein DnaJ; Provisional
 209-272 2.15e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 237653 [Multi-domain]  Cd Length: 380  Bit Score: 43.15  E-value: 2.15e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 330254382 209 DVVCPTCNADG-EPGFYKENqmmkCSTCYGRGLVAHKDGS-------DTICTNCNGKGKL---PCPTCQSRGLIK 272
Cdd:PRK14276 146 EATCHTCNGSGaKPGTSPVT----CGKCHGSGVITVDTQTplgmmrrQVTCDVCHGTGKEikePCQTCHGTGHEK 216
PRK14295 PRK14295
molecular chaperone DnaJ;
187-280 2.50e-04

molecular chaperone DnaJ;


Pssm-ID: 237665 [Multi-domain]  Cd Length: 389  Bit Score: 42.91  E-value: 2.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254382 187 ETQVLVPNSETVEKCT-GCTGRGDVVCPTCNADGEpgfyKENQMMK-CSTCYGRGLVAHKDGSDTICTncngkgklPCPT 264
Cdd:PRK14295 143 ESEVTLSFTEAIDGATvPLRLTSQAPCPACSGTGA----KNGTTPRvCPTCSGTGQVSRNSGGFSLSE--------PCPD 210

                         90
                 ....*....|....*....
gi 330254382 265 CQSRGLI---KCQTCDSTG 280
Cdd:PRK14295 211 CKGRGLIaddPCLVCKGSG 229
DnaJ_zf cd10719
Zinc finger domain of DnaJ and HSP40; Central/middle or CxxCxGxG-motif containing domain of ...
 232-280 3.31e-04

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: 38.78  E-value: 3.31e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 330254382 232 CSTCYGRGlvAHKDGSDTICTNCNGKGKL---------------PCPTCQSRGLI---KCQTCDSTG 280
Cdd:cd10719    1 CPTCNGSG--AKPGTKPKTCPTCGGSGQVrqvqgtgfgffqtqtTCPTCGGTGKIikdPCPKCKGKG 65
PTZ00037 PTZ00037
DnaJ_C chaperone protein; Provisional
 209-290 3.36e-04

DnaJ_C chaperone protein; Provisional


Pssm-ID: 240236 [Multi-domain]  Cd Length: 421  Bit Score: 42.50  E-value: 3.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254382 209 DVVCPTCNADGEPgfykENQMMKCSTCYGRGL---------VAHKdgSDTICTNCNGKGK-LPcptcQSRgliKCQTCDS 278
Cdd:PTZ00037 150 DVICANCEGHGGP----KDAFVDCKLCNGQGIrvqirqmgsMIHQ--TQSTCNSCNGQGKiIP----ESK---KCKNCSG 216

                         90
                 ....*....|..
gi 330254382 279 TGSLLTSSIAVV 290
Cdd:PTZ00037 217 KGVKKTRKILEV 228
PLN03165 PLN03165
chaperone protein dnaJ-related; Provisional
 231-270 3.47e-04

chaperone protein dnaJ-related; Provisional


Pssm-ID: 178709 [Multi-domain]  Cd Length: 111  Bit Score: 39.80  E-value: 3.47e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 330254382 231 KCSTCYGRGLVAHKDGSD----TICTNCNGKGKLPCPTCQSRGL 270
Cdd:PLN03165  54 VCRFCVGSGNVTVELGGGekevSKCINCDGAGSLTCTTCQGSGI 97
PRK14296 PRK14296
chaperone protein DnaJ; Provisional
 198-259 3.88e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 237666 [Multi-domain]  Cd Length: 372  Bit Score: 42.24  E-value: 3.88e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 330254382 198 VEKCTGCTGRG-----DV-VCPTCNADGE------PGFYKENQMMKCSTCYGRGLVAHKDgsdtiCTNCNGKGK 259
Cdd:PRK14296 149 LTNCSKCFGSGaesnsDIhICNNCHGTGEvlvqknMGFFQFQQSAKCNVCNGAGKIIKNK-----CKNCKGKGK 217
PRK14285 PRK14285
chaperone protein DnaJ; Provisional
 224-282 4.24e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 172773 [Multi-domain]  Cd Length: 365  Bit Score: 42.29  E-value: 4.24e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 330254382 224 YKEN----QMMKCSTCYGRGlvAHKDGSDTICTNCNGKGKL-----------PCPTCQSRGLI---KCQTCDSTGSL 282
Cdd:PRK14285 137 YKNNinitRNMLCESCLGKK--SEKGTSPSICNMCNGSGRVmqgggffrvttTCPKCYGNGKIisnPCKSCKGKGSL 211
PRK14286 PRK14286
chaperone protein DnaJ; Provisional
 228-280 5.75e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 172774 [Multi-domain]  Cd Length: 372  Bit Score: 41.90  E-value: 5.75e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 330254382 228 QMMKCSTCYGRGlvAHKDGSDTICTNCNGKGKL-----------PCPTCQSRGLI---KCQTCDSTG 280
Cdd:PRK14286 149 RLESCVDCNGSG--ASKGSSPTTCPDCGGSGQIrrtqgffsvatTCPTCRGKGTVisnPCKTCGGQG 213
PRK14284 PRK14284
chaperone protein DnaJ; Provisional
 187-272 1.45e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 237658 [Multi-domain]  Cd Length: 391  Bit Score: 40.60  E-value: 1.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254382 187 ETQVLVPNSETvekCTGCTGRGdvvcpTCNADGepgfykenqMMKCSTCYGRGLVAHKDG---SDTICTNCNGKGKL--- 260
Cdd:PRK14284 150 EKELLVSGYKS---CDACSGSG-----ANSSQG---------IKVCDRCKGSGQVVQSRGffsMASTCPECGGEGRVitd 212

                         90
                 ....*....|..
gi 330254382 261 PCPTCQSRGLIK 272
Cdd:PRK14284 213 PCSVCRGQGRIK 224
PRK14291 PRK14291
chaperone protein DnaJ; Provisional
 192-258 1.71e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 237661 [Multi-domain]  Cd Length: 382  Bit Score: 40.52  E-value: 1.71e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 330254382 192 VPNSETVEKCTGC---TGRGDVVCPTCNADGE----PGFYKENQmmKCSTCYGRGLVAHKdgsdtiCTNCNGKG 258
Cdd:PRK14291 153 VPRYVPCEACGGTgydPGSGEKVCPTCGGSGEiyqrGGFFRISQ--TCPTCGGEGVLREP------CSKCNGRG 218
PRK14281 PRK14281
chaperone protein DnaJ; Provisional
 210-270 1.73e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 237657 [Multi-domain]  Cd Length: 397  Bit Score: 40.18  E-value: 1.73e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 330254382 210 VVCPTCNADGEpgfyKENQMMKCSTCYGRGLVahKDGSDTI---------CTNCNGKGKL---PCPTCQSRGL 270
Cdd:PRK14281 164 VPCKECNGTGS----KTGATETCPTCHGSGEV--RQASKTMfgqfvnitaCPTCGGEGRVvkdRCPACYGEGI 230
PRK14293 PRK14293
molecular chaperone DnaJ;
232-280 1.95e-03

molecular chaperone DnaJ;


Pssm-ID: 237663 [Multi-domain]  Cd Length: 374  Bit Score: 39.97  E-value: 1.95e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 330254382 232 CSTCYGRGLvahKDGSD-TICTNCNGKGKL---------------PCPTCQSRGLI---KCQTCDSTG 280
Cdd:PRK14293 146 CETCRGSGA---KPGTGpTTCSTCGGAGQVrratrtpfgsftqvsECPTCNGTGQViedPCDACGGQG 210
PRK14287 PRK14287
chaperone protein DnaJ; Provisional
 186-272 2.25e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 237659 [Multi-domain]  Cd Length: 371  Bit Score: 39.99  E-value: 2.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254382 186 KETQVLVPNSETVEKCTGCTGRGDVVCPTCNADGEPGFYKENQmmkcSTCYGRglVAHKdgsdTICTNCNGKGKL---PC 262
Cdd:PRK14287 129 KETEIEIPREETCGTCHGSGAKPGTKPETCSHCGGSGQLNVEQ----NTPFGR--VVNR----RVCHHCEGTGKIikqKC 198

                         90
                 ....*....|
gi 330254382 263 PTCQSRGLIK 272
Cdd:PRK14287 199 ATCGGKGKVR 208
DnaJ_C pfam01556
DnaJ C terminal domain; This family consists of the C terminal region of the DnaJ protein. It ...
 209-275 2.64e-03

DnaJ C terminal domain; This family consists of the C terminal region of the DnaJ protein. It is always found associated with pfam00226 and pfam00684. DnaJ is a chaperone associated with the Hsp70 heat-shock system involved in protein folding and renaturation after stress. The two C-terminal domains CTDI and CTDII, both incorporated in this family are necessary for maintaining the J-domains in their specific relative positions. Structural analysis of PDB:1nlt shows that PF00684 is nested within this DnaJ C-terminal region.


Pssm-ID: 460251 [Multi-domain]  Cd Length: 213  Bit Score: 39.16  E-value: 2.64e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 330254382  209 DVVCPTCNADG-EPGfykeNQMMKCSTCYGRGLVAHKDGSDTICTNCNGKG------KLPCPTCQSRGLIKCQT 275
Cdd:pfam01556  25 NVICDTCGGSGaKPG----TSPKTCPCCGGGGQVRRQFGFFSTCTCCPCCGgggkiiDKCCKCCGGGGVVEKKT 94
PRK14280 PRK14280
molecular chaperone DnaJ;
186-241 2.84e-03

molecular chaperone DnaJ;


Pssm-ID: 237656 [Multi-domain]  Cd Length: 376  Bit Score: 39.70  E-value: 2.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330254382 186 KETQVLVPNSETVEKCTG--------------CTGRGDV---------------VCPTCNADGEpgFYKEnqmmKCSTCY 236
Cdd:PRK14280 134 KEKEIEIPKEETCDTCHGsgakpgtsketcshCGGSGQVsveqntpfgrvvnrqTCPHCNGTGQ--EIKE----KCPTCH 207


                 ....*
gi 330254382 237 GRGLV 241
Cdd:PRK14280 208 GKGKV 212
PRK14279 PRK14279
molecular chaperone DnaJ;
201-269 3.60e-03

molecular chaperone DnaJ;


Pssm-ID: 237655 [Multi-domain]  Cd Length: 392  Bit Score: 39.33  E-value: 3.60e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 330254382 201 CTGCTGRGD------VVCPTCNADgepGFYKENQmmkcstcygrGLVahkdGSDTICTNCNGKGKL---PCPTCQSRG 269
Cdd:PRK14279 176 CTTCHGSGArpgtspKVCPTCNGS---GVISRNQ----------GAF----GFSEPCTDCRGTGSIiedPCEECKGTG 236
PRK14301 PRK14301
chaperone protein DnaJ; Provisional
 209-280 6.10e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 237668 [Multi-domain]  Cd Length: 373  Bit Score: 38.57  E-value: 6.10e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 330254382 209 DVVCPTCNADG-EPGFYKENqmmkCSTCYGRGLVAHKDGSDTICTncngkgklPCPTCQSRGLI---KCQTCDSTG 280
Cdd:PRK14301 144 NVTCDDCGGSGaAPGTSPET----CRHCGGSGQVRQSQGFFQIAV--------PCPVCRGEGRVithPCPKCKGSG 207
PRK14278 PRK14278
chaperone protein DnaJ; Provisional
 232-280 7.98e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 237654 [Multi-domain]  Cd Length: 378  Bit Score: 38.11  E-value: 7.98e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 330254382 232 CSTCYGRGlvAHKDGSDTICTNCNGKGKL---------------PCPTCQSRGLI---KCQTCDSTG 280
Cdd:PRK14278 142 CDRCHGKG--TAGDSKPVTCDTCGGRGEVqtvqrsflgqvmtsrPCPTCRGVGEVipdPCHECAGDG 206
 
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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