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Conserved domains on  [gi|1034633632|ref|XP_016862013|]
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protein SSUH2 homolog isoform X7 [Homo sapiens]

Protein Classification

DnaJ_zf domain-containing protein( domain architecture ID 10180502)

DnaJ_zf domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DnaJ_zf cd10719
Zinc finger domain of DnaJ and HSP40; Central/middle or CxxCxGxG-motif containing domain of ...
 319-386 5.42e-07

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: 46.87  E-value: 5.42e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034633632 319 CHKCHGRG------RYKCSGCHGAGTVRcpsccgakrkakQSRRCQLCAGSGRRRCSTCSGRG---NKTCATCKGEK 386
Cdd:cd10719     1 CPTCNGSGakpgtkPKTCPTCGGSGQVR------------QVQGTGFGFFQTQTTCPTCGGTGkiiKDPCPKCKGKG 65
 
Name Accession Description Interval E-value
DnaJ_zf cd10719
Zinc finger domain of DnaJ and HSP40; Central/middle or CxxCxGxG-motif containing domain of ...
 319-386 5.42e-07

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: 46.87  E-value: 5.42e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034633632 319 CHKCHGRG------RYKCSGCHGAGTVRcpsccgakrkakQSRRCQLCAGSGRRRCSTCSGRG---NKTCATCKGEK 386
Cdd:cd10719     1 CPTCNGSGakpgtkPKTCPTCGGSGQVR------------QVQGTGFGFFQTQTTCPTCGGTGkiiKDPCPKCKGKG 65
DnaJ_CXXCXGXG pfam00684
DnaJ central domain; The central cysteine-rich (CR) domain of DnaJ proteins contains four ...
 319-386 5.42e-06

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: 44.09  E-value: 5.42e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034633632 319 CHKCHGRG------RYKCSGCHGAGTVRcpsccgakrkakQSRRCQLCAGSGRRRCSTCSGRG---NKTCATCKGEK 386
Cdd:pfam00684   1 CPTCNGSGakpgtkPTTCPTCGGTGQVR------------RVQQTGPGFFQMQSTCPTCGGTGkiiKDPCKKCKGKG 65
PLN03165 PLN03165
chaperone protein dnaJ-related; Provisional
 319-375 2.39e-05

chaperone protein dnaJ-related; Provisional


Pssm-ID: 178709 [Multi-domain]  Cd Length: 111  Bit Score: 43.65  E-value: 2.39e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034633632 319 CHKCHGRGRYKCSGCHGAGTVRCPSCCGAKRKAKqsrrCQLCAGSGRRRCSTCSGRG 375
Cdd:PLN03165   44 CFPCSGTGAQVCRFCVGSGNVTVELGGGEKEVSK----CINCDGAGSLTCTTCQGSG 96
 
Name Accession Description Interval E-value
DnaJ_zf cd10719
Zinc finger domain of DnaJ and HSP40; Central/middle or CxxCxGxG-motif containing domain of ...
 319-386 5.42e-07

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: 46.87  E-value: 5.42e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034633632 319 CHKCHGRG------RYKCSGCHGAGTVRcpsccgakrkakQSRRCQLCAGSGRRRCSTCSGRG---NKTCATCKGEK 386
Cdd:cd10719     1 CPTCNGSGakpgtkPKTCPTCGGSGQVR------------QVQGTGFGFFQTQTTCPTCGGTGkiiKDPCPKCKGKG 65
DnaJ_CXXCXGXG pfam00684
DnaJ central domain; The central cysteine-rich (CR) domain of DnaJ proteins contains four ...
 319-386 5.42e-06

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: 44.09  E-value: 5.42e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034633632 319 CHKCHGRG------RYKCSGCHGAGTVRcpsccgakrkakQSRRCQLCAGSGRRRCSTCSGRG---NKTCATCKGEK 386
Cdd:pfam00684   1 CPTCNGSGakpgtkPTTCPTCGGTGQVR------------RVQQTGPGFFQMQSTCPTCGGTGkiiKDPCKKCKGKG 65
PLN03165 PLN03165
chaperone protein dnaJ-related; Provisional
 319-375 2.39e-05

chaperone protein dnaJ-related; Provisional


Pssm-ID: 178709 [Multi-domain]  Cd Length: 111  Bit Score: 43.65  E-value: 2.39e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034633632 319 CHKCHGRGRYKCSGCHGAGTVRCPSCCGAKRKAKqsrrCQLCAGSGRRRCSTCSGRG 375
Cdd:PLN03165   44 CFPCSGTGAQVCRFCVGSGNVTVELGGGEKEVSK----CINCDGAGSLTCTTCQGSG 96
PRK14280 PRK14280
molecular chaperone DnaJ;
318-378 5.34e-05

molecular chaperone DnaJ;


Pssm-ID: 237656 [Multi-domain]  Cd Length: 376  Bit Score: 45.48  E-value: 5.34e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633632 318 ECHKCHGRG------RYKCSGCHGAGTVRCPSCCGAKRKAKQsRRCQLCAGSGR---RRCSTCSGRGNKT 378
Cdd:PRK14280  145 TCDTCHGSGakpgtsKETCSHCGGSGQVSVEQNTPFGRVVNR-QTCPHCNGTGQeikEKCPTCHGKGKVR 213
PRK14276 PRK14276
chaperone protein DnaJ; Provisional
 318-375 1.49e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 237653 [Multi-domain]  Cd Length: 380  Bit Score: 43.92  E-value: 1.49e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034633632 318 ECHKCHGRGRYK------CSGCHGAG--TVRCPSCCGAKRkakQSRRCQLCAGSG---RRRCSTCSGRG 375
Cdd:PRK14276  148 TCHTCNGSGAKPgtspvtCGKCHGSGviTVDTQTPLGMMR---RQVTCDVCHGTGkeiKEPCQTCHGTG 213
DnaJ_C pfam01556
DnaJ C terminal domain; This family consists of the C terminal region of the DnaJ protein. It ...
 305-370 1.84e-04

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: 43.01  E-value: 1.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633632 305 TRKFQVPHsslVKECHKCHGRG------RYKCSGCHGAGTVR----------CPSCCGAKRKAKqSRRCQLCAGSGRRRC 368
Cdd:pfam01556  17 TKKIKITR---NVICDTCGGSGakpgtsPKTCPCCGGGGQVRrqfgffstctCCPCCGGGGKII-DKCCKCCGGGGVVEK 92


                  ..
gi 1034633632 369 ST 370
Cdd:pfam01556  93 KT 94
PRK14283 PRK14283
chaperone protein DnaJ; Provisional
 274-385 2.27e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 184604 [Multi-domain]  Cd Length: 378  Bit Score: 43.66  E-value: 2.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633632 274 FTNHSVDGPQRGAsprlwDIKVQGPPMFQED----TRKFQVPHSslvKECHKCHGrGRYKcsgcHGAGTVRCPSCCGAKr 349
Cdd:PRK14283  108 FGGGSRHGPQRGA-----DIYTEVEITLEEAasgvEKDIKVRHT---KKCPVCNG-SRAE----PGSEVKTCPTCGGTG- 173

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1034633632 350 KAKQSRRCQLCAGSGRRRCSTCSGRGN---KTCATCKGE 385
Cdd:PRK14283  174 QVKQVRNTILGQMMNVTTCPDCQGEGKiveKPCSNCHGK 212
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
 281-387 2.68e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 43.30  E-value: 2.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633632 281 GPQRGASPRlWDIKVQgppmFQE----DTRKFQVPHSslvKECHKCHGRGRYKcsgchGAGTVRCPSCcGAKRKAKQSRR 356
Cdd:PRK14298  110 GPRRGSDLR-YDLYIT----LEEaafgVRKDIDVPRA---ERCSTCSGTGAKP-----GTSPKRCPTC-GGTGQVTTTRS 175

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1034633632 357 CQLCAGSGRRRCSTCSGRGN---KTCATCKGEKK 387
Cdd:PRK14298  176 TPLGQFVTTTTCSTCHGRGQvieSPCPVCSGTGK 209
PRK14296 PRK14296
chaperone protein DnaJ; Provisional
 315-375 3.56e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 237666 [Multi-domain]  Cd Length: 372  Bit Score: 43.01  E-value: 3.56e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633632 315 LVKECHKCHGRGRYK------CSGCHGAGTVRCPSCCGAkRKAKQSRRCQLCAGSG---RRRCSTCSGRG 375
Cdd:PRK14296  148 LLTNCSKCFGSGAESnsdihiCNNCHGTGEVLVQKNMGF-FQFQQSAKCNVCNGAGkiiKNKCKNCKGKG 216
PRK14287 PRK14287
chaperone protein DnaJ; Provisional
 300-375 4.42e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 237659 [Multi-domain]  Cd Length: 371  Bit Score: 42.69  E-value: 4.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633632 300 MFQEDTrKFQVPHSslvKECHKCHGRGRY------KCSGCHGAGTVRCPSCCGAKRKAKQsRRCQLCAGSGR---RRCST 370
Cdd:PRK14287  126 VFGKET-EIEIPRE---ETCGTCHGSGAKpgtkpeTCSHCGGSGQLNVEQNTPFGRVVNR-RVCHHCEGTGKiikQKCAT 200


                  ....*
gi 1034633632 371 CSGRG 375
Cdd:PRK14287  201 CGGKG 205
PRK14282 PRK14282
chaperone protein DnaJ; Provisional
 317-367 4.98e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 184603 [Multi-domain]  Cd Length: 369  Bit Score: 42.47  E-value: 4.98e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034633632 317 KECHKCHGRG------RYKCSGCHGAGTVR---------------CPSCCGAKRKAKQSrrCQLCAGSGRRR 367
Cdd:PRK14282  153 ETCPHCGGTGvepgsgYVTCPKCHGTGRIReerrsffgvfvsertCERCGGTGKIPGEY--CHECGGSGRIR 222
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 319-340 8.39e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 41.67  E-value: 8.39e-04
                          10        20
                  ....*....|....*....|....*
gi 1034633632 319 CHKCHGRGRY---KCSGCHGAGTVR 340
Cdd:PRK10767  184 CPTCHGRGKIikdPCKKCHGQGRVE 208
PRK14281 PRK14281
chaperone protein DnaJ; Provisional
 307-367 8.82e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 237657 [Multi-domain]  Cd Length: 397  Bit Score: 41.72  E-value: 8.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034633632 307 KFQVPhsslvkeCHKCHGRGRYK-----CSGCHGAGTVR---------------CPSCCGAKRKAKQsrRCQLCAGSGRR 366
Cdd:PRK14281  161 KKQVP-------CKECNGTGSKTgatetCPTCHGSGEVRqasktmfgqfvnitaCPTCGGEGRVVKD--RCPACYGEGIK 231


                  .
gi 1034633632 367 R 367
Cdd:PRK14281  232 Q 232
PRK14290 PRK14290
chaperone protein DnaJ; Provisional
 316-339 7.26e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 172778 [Multi-domain]  Cd Length: 365  Bit Score: 38.76  E-value: 7.26e-03
                          10        20
                  ....*....|....*....|....*..
gi 1034633632 316 VKECHKCHGRGRY---KCSGCHGAGTV 339
Cdd:PRK14290  191 VTTCRTCGGRGRIpeeKCPRCNGTGTV 217
 
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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