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Conserved domains on  [gi|376334943|ref|NP_001243677|]
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protein SSUH2 homolog isoform 1 [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 ...
 177-244 1.56e-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: 48.02  E-value: 1.56e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 376334943 177 CHKCHGRG------RYKCSGCHGAGTVRcpsccgakrkakQSRRCQLCAGSGRRRCSTCSGRG---NKTCATCKGEK 244
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 ...
 177-244 1.56e-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: 48.02  E-value: 1.56e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 376334943 177 CHKCHGRG------RYKCSGCHGAGTVRcpsccgakrkakQSRRCQLCAGSGRRRCSTCSGRG---NKTCATCKGEK 244
Cdd:cd10719    1 CPTCNGSGakpgtkPKTCPTCGGSGQVR------------QVQGTGFGFFQTQTTCPTCGGTGkiiKDPCPKCKGKG 65
DnaJ_CXXCXGXG pfam00684
DnaJ central domain; The central cysteine-rich (CR) domain of DnaJ proteins contains four ...
 177-244 1.62e-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: 44.86  E-value: 1.62e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 376334943  177 CHKCHGRG------RYKCSGCHGAGTVRcpsccgakrkakQSRRCQLCAGSGRRRCSTCSGRG---NKTCATCKGEK 244
Cdd:pfam00684   1 CPTCNGSGakpgtkPTTCPTCGGTGQVR------------RVQQTGPGFFQMQSTCPTCGGTGkiiKDPCKKCKGKG 65
PLN03165 PLN03165
chaperone protein dnaJ-related; Provisional
 177-233 1.79e-05

chaperone protein dnaJ-related; Provisional


Pssm-ID: 178709 [Multi-domain]  Cd Length: 111  Bit Score: 43.27  E-value: 1.79e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 376334943 177 CHKCHGRGRYKCSGCHGAGTVRCPSCCGAKRKAKqsrrCQLCAGSGRRRCSTCSGRG 233
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 ...
 177-244 1.56e-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: 48.02  E-value: 1.56e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 376334943 177 CHKCHGRG------RYKCSGCHGAGTVRcpsccgakrkakQSRRCQLCAGSGRRRCSTCSGRG---NKTCATCKGEK 244
Cdd:cd10719    1 CPTCNGSGakpgtkPKTCPTCGGSGQVR------------QVQGTGFGFFQTQTTCPTCGGTGkiiKDPCPKCKGKG 65
DnaJ_CXXCXGXG pfam00684
DnaJ central domain; The central cysteine-rich (CR) domain of DnaJ proteins contains four ...
 177-244 1.62e-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: 44.86  E-value: 1.62e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 376334943  177 CHKCHGRG------RYKCSGCHGAGTVRcpsccgakrkakQSRRCQLCAGSGRRRCSTCSGRG---NKTCATCKGEK 244
Cdd:pfam00684   1 CPTCNGSGakpgtkPTTCPTCGGTGQVR------------RVQQTGPGFFQMQSTCPTCGGTGkiiKDPCKKCKGKG 65
PLN03165 PLN03165
chaperone protein dnaJ-related; Provisional
 177-233 1.79e-05

chaperone protein dnaJ-related; Provisional


Pssm-ID: 178709 [Multi-domain]  Cd Length: 111  Bit Score: 43.27  E-value: 1.79e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 376334943 177 CHKCHGRGRYKCSGCHGAGTVRCPSCCGAKRKAKqsrrCQLCAGSGRRRCSTCSGRG 233
Cdd:PLN03165  44 CFPCSGTGAQVCRFCVGSGNVTVELGGGEKEVSK----CINCDGAGSLTCTTCQGSG 96
PRK14280 PRK14280
molecular chaperone DnaJ;
176-236 3.22e-05

molecular chaperone DnaJ;


Pssm-ID: 237656 [Multi-domain]  Cd Length: 376  Bit Score: 45.48  E-value: 3.22e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 376334943 176 ECHKCHGRG------RYKCSGCHGAGTVRCPSCCGAKRKAKQsRRCQLCAGSGR---RRCSTCSGRGNKT 236
Cdd:PRK14280 145 TCDTCHGSGakpgtsKETCSHCGGSGQVSVEQNTPFGRVVNR-QTCPHCNGTGQeikEKCPTCHGKGKVR 213
PRK14276 PRK14276
chaperone protein DnaJ; Provisional
 176-233 9.09e-05

chaperone protein DnaJ; Provisional


Pssm-ID: 237653 [Multi-domain]  Cd Length: 380  Bit Score: 43.92  E-value: 9.09e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 376334943 176 ECHKCHGRGRYK------CSGCHGAG--TVRCPSCCGAKRkakQSRRCQLCAGSG---RRRCSTCSGRG 233
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 ...
 163-228 1.06e-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: 1.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 376334943  163 TRKFQVPHsslVKECHKCHGRG------RYKCSGCHGAGTVR----------CPSCCGAKRKAKqSRRCQLCAGSGRRRC 226
Cdd:pfam01556  17 TKKIKITR---NVICDTCGGSGakpgtsPKTCPCCGGGGQVRrqfgffstctCCPCCGGGGKII-DKCCKCCGGGGVVEK 92


                  ..
gi 376334943  227 ST 228
Cdd:pfam01556  93 KT 94
PRK14283 PRK14283
chaperone protein DnaJ; Provisional
 132-243 1.39e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 184604 [Multi-domain]  Cd Length: 378  Bit Score: 43.66  E-value: 1.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 376334943 132 FTNHSVDGPQRGAsprlwDIKVQGPPMFQED----TRKFQVPHSslvKECHKCHGrGRYKcsgcHGAGTVRCPSCCGAKr 207
Cdd:PRK14283 108 FGGGSRHGPQRGA-----DIYTEVEITLEEAasgvEKDIKVRHT---KKCPVCNG-SRAE----PGSEVKTCPTCGGTG- 173

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 376334943 208 KAKQSRRCQLCAGSGRRRCSTCSGRGN---KTCATCKGE 243
Cdd:PRK14283 174 QVKQVRNTILGQMMNVTTCPDCQGEGKiveKPCSNCHGK 212
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
 139-245 1.64e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 43.30  E-value: 1.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 376334943 139 GPQRGASPRlWDIKVQgppmFQE----DTRKFQVPHSslvKECHKCHGRGRYKcsgchGAGTVRCPSCcGAKRKAKQSRR 214
Cdd:PRK14298 110 GPRRGSDLR-YDLYIT----LEEaafgVRKDIDVPRA---ERCSTCSGTGAKP-----GTSPKRCPTC-GGTGQVTTTRS 175

                         90       100       110
                 ....*....|....*....|....*....|....
gi 376334943 215 CQLCAGSGRRRCSTCSGRGN---KTCATCKGEKK 245
Cdd:PRK14298 176 TPLGQFVTTTTCSTCHGRGQvieSPCPVCSGTGK 209
PRK14296 PRK14296
chaperone protein DnaJ; Provisional
 173-233 2.19e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 237666 [Multi-domain]  Cd Length: 372  Bit Score: 43.01  E-value: 2.19e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 376334943 173 LVKECHKCHGRGRYK------CSGCHGAGTVRCPSCCGAkRKAKQSRRCQLCAGSG---RRRCSTCSGRG 233
Cdd:PRK14296 148 LLTNCSKCFGSGAESnsdihiCNNCHGTGEVLVQKNMGF-FQFQQSAKCNVCNGAGkiiKNKCKNCKGKG 216
PRK14287 PRK14287
chaperone protein DnaJ; Provisional
 158-233 2.35e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 237659 [Multi-domain]  Cd Length: 371  Bit Score: 42.69  E-value: 2.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 376334943 158 MFQEDTrKFQVPHSslvKECHKCHGRGRY------KCSGCHGAGTVRCPSCCGAKRKAKQsRRCQLCAGSGR---RRCST 228
Cdd:PRK14287 126 VFGKET-EIEIPRE---ETCGTCHGSGAKpgtkpeTCSHCGGSGQLNVEQNTPFGRVVNR-RVCHHCEGTGKiikQKCAT 200


                 ....*
gi 376334943 229 CSGRG 233
Cdd:PRK14287 201 CGGKG 205
PRK14282 PRK14282
chaperone protein DnaJ; Provisional
 175-225 5.31e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 184603 [Multi-domain]  Cd Length: 369  Bit Score: 41.70  E-value: 5.31e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 376334943 175 KECHKCHGRG------RYKCSGCHGAGTVR---------------CPSCCGAKRKAKQSrrCQLCAGSGRRR 225
Cdd:PRK14282 153 ETCPHCGGTGvepgsgYVTCPKCHGTGRIReerrsffgvfvsertCERCGGTGKIPGEY--CHECGGSGRIR 222
PRK14281 PRK14281
chaperone protein DnaJ; Provisional
 165-225 5.45e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 237657 [Multi-domain]  Cd Length: 397  Bit Score: 41.72  E-value: 5.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 376334943 165 KFQVPhsslvkeCHKCHGRGRYK-----CSGCHGAGTVR---------------CPSCCGAKRKAKQsrRCQLCAGSGRR 224
Cdd:PRK14281 161 KKQVP-------CKECNGTGSKTgatetCPTCHGSGEVRqasktmfgqfvnitaCPTCGGEGRVVKD--RCPACYGEGIK 231


                 .
gi 376334943 225 R 225
Cdd:PRK14281 232 Q 232
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 177-198 6.03e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 41.67  E-value: 6.03e-04
                         10        20
                 ....*....|....*....|....*
gi 376334943 177 CHKCHGRGRY---KCSGCHGAGTVR 198
Cdd:PRK10767 184 CPTCHGRGKIikdPCKKCHGQGRVE 208
PRK14277 PRK14277
chaperone protein DnaJ; Provisional
 139-247 1.51e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 184599 [Multi-domain]  Cd Length: 386  Bit Score: 40.17  E-value: 1.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 376334943 139 GPQRGAsprlwDIKVQGPPMFQEDTrkFQVPHSSLVKechkchgrgRY-KCSGCHGAGTvrcpsccgakRKAKQSRRCQL 217
Cdd:PRK14277 124 GPQKGA-----DIRYDLELTFEEAA--FGTEKEIEVE---------RFeKCDVCKGSGA----------KPGSKPVTCPV 177

                         90       100       110
                 ....*....|....*....|....*....|....
gi 376334943 218 CAGSG--RRRCSTCSGR--GNKTCATCKGEKKLL 247
Cdd:PRK14277 178 CHGTGqvRTRQNTPFGRivNIRTCDRCHGEGKII 211
PRK14290 PRK14290
chaperone protein DnaJ; Provisional
 174-197 4.59e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 172778 [Multi-domain]  Cd Length: 365  Bit Score: 38.76  E-value: 4.59e-03
                         10        20
                 ....*....|....*....|....*..
gi 376334943 174 VKECHKCHGRGRY---KCSGCHGAGTV 197
Cdd:PRK14290 191 VTTCRTCGGRGRIpeeKCPRCNGTGTV 217
PRK14290 PRK14290
chaperone protein DnaJ; Provisional
 199-242 4.93e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 172778 [Multi-domain]  Cd Length: 365  Bit Score: 38.76  E-value: 4.93e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 376334943 199 CPSCCGAKRKAKQSRRCQLCAGSGRRR---------------CSTCSGRG---NKTCATCKG 242
Cdd:PRK14290 152 CPDCSGTGAKNGKLITCPTCHGTGQQRivrgqgffrmvtvttCRTCGGRGripEEKCPRCNG 213
DnaJ_CXXCXGXG pfam00684
DnaJ central domain; The central cysteine-rich (CR) domain of DnaJ proteins contains four ...
 174-206 9.88e-03

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: 34.46  E-value: 9.88e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 376334943  174 VKECHKCHGRGRYK---------------CSGCHGAGTV---RCPSCCGAK 206
Cdd:pfam00684  15 PTTCPTCGGTGQVRrvqqtgpgffqmqstCPTCGGTGKIikdPCKKCKGKG 65
 
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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