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Conserved domains on  [gi|2026616585|ref|NP_057015|]
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protein SSUH2 homolog isoform 2 [Homo sapiens]

Protein Classification

J domain-containing protein( domain architecture ID 230175)

J domain-containing protein similar to cauliflower (Brassica oleracea var botrytis) DnaJ cysteine-rich domain-containing protein encoded by Orange (Or) gene mutation that mediates high levels of beta-carotene accumulation

Gene Ontology:  GO:0006457
PubMed:  9585179|23894646|15170475

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DnaJ_zf super family cl21539
Zinc finger domain of DnaJ and HSP40; Central/middle or CxxCxGxG-motif containing domain of ...
 104-171 2.15e-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.


The actual alignment was detected with superfamily member cd10719:

Pssm-ID: 473904 [Multi-domain]  Cd Length: 65  Bit Score: 44.55  E-value: 2.15e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2026616585 104 CHKCHGRG------RYKCSGCHGAGTVRcpsccgakrkakQSRRCQLCAGSGRRRCSTCSGRG---NKTCATCKGEK 171
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 ...
 104-171 2.15e-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: 44.55  E-value: 2.15e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2026616585 104 CHKCHGRG------RYKCSGCHGAGTVRcpsccgakrkakQSRRCQLCAGSGRRRCSTCSGRG---NKTCATCKGEK 171
Cdd:cd10719     1 CPTCNGSGakpgtkPKTCPTCGGSGQVR------------QVQGTGFGFFQTQTTCPTCGGTGkiiKDPCPKCKGKG 65
PRK14293 PRK14293
molecular chaperone DnaJ;
66-152 4.86e-06

molecular chaperone DnaJ;


Pssm-ID: 237663 [Multi-domain]  Cd Length: 374  Bit Score: 47.29  E-value: 4.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026616585  66 GPQRGASPRLwDIKVQgppmFQE----DTRKFQVPHsslVKECHKCHGRGRYK------CSGCHGAGTVR---------- 125
Cdd:PRK14293  112 GPQRGDDLRY-DLKLD----FREaifgGEKEIRIPH---LETCETCRGSGAKPgtgpttCSTCGGAGQVRratrtpfgsf 183

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2026616585 126 -----CPSCCGAKRKAKQsrRCQLCAGSGRRR 152
Cdd:PRK14293  184 tqvseCPTCNGTGQVIED--PCDACGGQGVKQ 213
DnaJ_CXXCXGXG pfam00684
DnaJ central domain; The central cysteine-rich (CR) domain of DnaJ proteins contains four ...
 104-171 1.98e-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: 1.98e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2026616585 104 CHKCHGRG------RYKCSGCHGAGTVRcpsccgakrkakQSRRCQLCAGSGRRRCSTCSGRG---NKTCATCKGEK 171
Cdd:pfam00684   1 CPTCNGSGakpgtkPTTCPTCGGTGQVR------------RVQQTGPGFFQMQSTCPTCGGTGkiiKDPCKKCKGKG 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 ...
 104-171 2.15e-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: 44.55  E-value: 2.15e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2026616585 104 CHKCHGRG------RYKCSGCHGAGTVRcpsccgakrkakQSRRCQLCAGSGRRRCSTCSGRG---NKTCATCKGEK 171
Cdd:cd10719     1 CPTCNGSGakpgtkPKTCPTCGGSGQVR------------QVQGTGFGFFQTQTTCPTCGGTGkiiKDPCPKCKGKG 65
PRK14293 PRK14293
molecular chaperone DnaJ;
66-152 4.86e-06

molecular chaperone DnaJ;


Pssm-ID: 237663 [Multi-domain]  Cd Length: 374  Bit Score: 47.29  E-value: 4.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026616585  66 GPQRGASPRLwDIKVQgppmFQE----DTRKFQVPHsslVKECHKCHGRGRYK------CSGCHGAGTVR---------- 125
Cdd:PRK14293  112 GPQRGDDLRY-DLKLD----FREaifgGEKEIRIPH---LETCETCRGSGAKPgtgpttCSTCGGAGQVRratrtpfgsf 183

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2026616585 126 -----CPSCCGAKRKAKQsrRCQLCAGSGRRR 152
Cdd:PRK14293  184 tqvseCPTCNGTGQVIED--PCDACGGQGVKQ 213
DnaJ_CXXCXGXG pfam00684
DnaJ central domain; The central cysteine-rich (CR) domain of DnaJ proteins contains four ...
 104-171 1.98e-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: 1.98e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2026616585 104 CHKCHGRG------RYKCSGCHGAGTVRcpsccgakrkakQSRRCQLCAGSGRRRCSTCSGRG---NKTCATCKGEK 171
Cdd:pfam00684   1 CPTCNGSGakpgtkPTTCPTCGGTGQVR------------RVQQTGPGFFQMQSTCPTCGGTGkiiKDPCKKCKGKG 65
PRK14280 PRK14280
molecular chaperone DnaJ;
103-163 2.13e-05

molecular chaperone DnaJ;


Pssm-ID: 237656 [Multi-domain]  Cd Length: 376  Bit Score: 45.48  E-value: 2.13e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026616585 103 ECHKCHGRG------RYKCSGCHGAGTVRCPSCCGAKRKAKQsRRCQLCAGSGR---RRCSTCSGRGNKT 163
Cdd:PRK14280  145 TCDTCHGSGakpgtsKETCSHCGGSGQVSVEQNTPFGRVVNR-QTCPHCNGTGQeikEKCPTCHGKGKVR 213
PLN03165 PLN03165
chaperone protein dnaJ-related; Provisional
 104-160 3.37e-05

chaperone protein dnaJ-related; Provisional


Pssm-ID: 178709 [Multi-domain]  Cd Length: 111  Bit Score: 42.50  E-value: 3.37e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2026616585 104 CHKCHGRGRYKCSGCHGAGTVRCPSCCGAKRKAKqsrrCQLCAGSGRRRCSTCSGRG 160
Cdd:PLN03165   44 CFPCSGTGAQVCRFCVGSGNVTVELGGGEKEVSK----CINCDGAGSLTCTTCQGSG 96
PRK14276 PRK14276
chaperone protein DnaJ; Provisional
 103-160 6.08e-05

chaperone protein DnaJ; Provisional


Pssm-ID: 237653 [Multi-domain]  Cd Length: 380  Bit Score: 43.92  E-value: 6.08e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2026616585 103 ECHKCHGRGRYK------CSGCHGAG--TVRCPSCCGAKRkakQSRRCQLCAGSG---RRRCSTCSGRG 160
Cdd:PRK14276  148 TCHTCNGSGAKPgtspvtCGKCHGSGviTVDTQTPLGMMR---RQVTCDVCHGTGkeiKEPCQTCHGTG 213
PRK14283 PRK14283
chaperone protein DnaJ; Provisional
 59-170 9.37e-05

chaperone protein DnaJ; Provisional


Pssm-ID: 184604 [Multi-domain]  Cd Length: 378  Bit Score: 43.66  E-value: 9.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026616585  59 FTNHSVDGPQRGAsprlwDIKVQGPPMFQED----TRKFQVPHSslvKECHKCHGrGRYKcsgcHGAGTVRCPSCCGAKr 134
Cdd:PRK14283  108 FGGGSRHGPQRGA-----DIYTEVEITLEEAasgvEKDIKVRHT---KKCPVCNG-SRAE----PGSEVKTCPTCGGTG- 173

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2026616585 135 KAKQSRRCQLCAGSGRRRCSTCSGRGN---KTCATCKGE 170
Cdd:PRK14283  174 QVKQVRNTILGQMMNVTTCPDCQGEGKiveKPCSNCHGK 212
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
 66-172 1.11e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 43.30  E-value: 1.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026616585  66 GPQRGASPRlWDIKVQgppmFQE----DTRKFQVPHSslvKECHKCHGRGRYKcsgchGAGTVRCPSCcGAKRKAKQSRR 141
Cdd:PRK14298  110 GPRRGSDLR-YDLYIT----LEEaafgVRKDIDVPRA---ERCSTCSGTGAKP-----GTSPKRCPTC-GGTGQVTTTRS 175

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2026616585 142 CQLCAGSGRRRCSTCSGRGN---KTCATCKGEKK 172
Cdd:PRK14298  176 TPLGQFVTTTTCSTCHGRGQvieSPCPVCSGTGK 209
PRK14287 PRK14287
chaperone protein DnaJ; Provisional
 85-160 1.43e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 237659 [Multi-domain]  Cd Length: 371  Bit Score: 43.07  E-value: 1.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026616585  85 MFQEDTrKFQVPHSslvKECHKCHGRGRY------KCSGCHGAGTVRCPSCCGAKRKAKQsRRCQLCAGSGR---RRCST 155
Cdd:PRK14287  126 VFGKET-EIEIPRE---ETCGTCHGSGAKpgtkpeTCSHCGGSGQLNVEQNTPFGRVVNR-RVCHHCEGTGKiikQKCAT 200


                  ....*
gi 2026616585 156 CSGRG 160
Cdd:PRK14287  201 CGGKG 205
PRK14296 PRK14296
chaperone protein DnaJ; Provisional
 100-160 1.48e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 237666 [Multi-domain]  Cd Length: 372  Bit Score: 43.01  E-value: 1.48e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026616585 100 LVKECHKCHGRGRYK------CSGCHGAGTVRCPSCCGAkRKAKQSRRCQLCAGSG---RRRCSTCSGRG 160
Cdd:PRK14296  148 LLTNCSKCFGSGAESnsdihiCNNCHGTGEVLVQKNMGF-FQFQQSAKCNVCNGAGkiiKNKCKNCKGKG 216
DnaJ_C pfam01556
DnaJ C terminal domain; This family consists of the C terminal region of the DnaJ protein. It ...
 90-155 2.44e-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: 41.47  E-value: 2.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026616585  90 TRKFQVPHsslVKECHKCHGRG------RYKCSGCHGAGTVR----------CPSCCGAKRKAKqSRRCQLCAGSGRRRC 153
Cdd:pfam01556  17 TKKIKITR---NVICDTCGGSGakpgtsPKTCPCCGGGGQVRrqfgffstctCCPCCGGGGKII-DKCCKCCGGGGVVEK 92


                  ..
gi 2026616585 154 ST 155
Cdd:pfam01556  93 KT 94
PRK14281 PRK14281
chaperone protein DnaJ; Provisional
 92-152 3.72e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 237657 [Multi-domain]  Cd Length: 397  Bit Score: 41.72  E-value: 3.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026616585  92 KFQVPhsslvkeCHKCHGRGRYK-----CSGCHGAGTVR---------------CPSCCGAKRKAKQsrRCQLCAGSGRR 151
Cdd:PRK14281  161 KKQVP-------CKECNGTGSKTgatetCPTCHGSGEVRqasktmfgqfvnitaCPTCGGEGRVVKD--RCPACYGEGIK 231


                  .
gi 2026616585 152 R 152
Cdd:PRK14281  232 Q 232
PRK14282 PRK14282
chaperone protein DnaJ; Provisional
 102-152 4.27e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 184603 [Multi-domain]  Cd Length: 369  Bit Score: 41.32  E-value: 4.27e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2026616585 102 KECHKCHGRG------RYKCSGCHGAGTVR---------------CPSCCGAKRKAKQSrrCQLCAGSGRRR 152
Cdd:PRK14282  153 ETCPHCGGTGvepgsgYVTCPKCHGTGRIReerrsffgvfvsertCERCGGTGKIPGEY--CHECGGSGRIR 222
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 104-125 5.34e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 41.28  E-value: 5.34e-04
                          10        20
                  ....*....|....*....|....*
gi 2026616585 104 CHKCHGRGRY---KCSGCHGAGTVR 125
Cdd:PRK10767  184 CPTCHGRGKIikdPCKKCHGQGRVE 208
PRK14277 PRK14277
chaperone protein DnaJ; Provisional
 66-174 1.04e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 184599 [Multi-domain]  Cd Length: 386  Bit Score: 40.17  E-value: 1.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026616585  66 GPQRGAsprlwDIKVQGPPMFQEDTrkFQVPHSSLVKechkchgrgRY-KCSGCHGAGTvrcpsccgakRKAKQSRRCQL 144
Cdd:PRK14277  124 GPQKGA-----DIRYDLELTFEEAA--FGTEKEIEVE---------RFeKCDVCKGSGA----------KPGSKPVTCPV 177

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2026616585 145 CAGSG--RRRCSTCSGR--GNKTCATCKGEKKLL 174
Cdd:PRK14277  178 CHGTGqvRTRQNTPFGRivNIRTCDRCHGEGKII 211
PRK14290 PRK14290
chaperone protein DnaJ; Provisional
 101-124 3.22e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 172778 [Multi-domain]  Cd Length: 365  Bit Score: 38.76  E-value: 3.22e-03
                          10        20
                  ....*....|....*....|....*..
gi 2026616585 101 VKECHKCHGRGRY---KCSGCHGAGTV 124
Cdd:PRK14290  191 VTTCRTCGGRGRIpeeKCPRCNGTGTV 217
PRK14290 PRK14290
chaperone protein DnaJ; Provisional
 126-169 3.46e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 172778 [Multi-domain]  Cd Length: 365  Bit Score: 38.76  E-value: 3.46e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2026616585 126 CPSCCGAKRKAKQSRRCQLCAGSGRRR---------------CSTCSGRG---NKTCATCKG 169
Cdd:PRK14290  152 CPDCSGTGAKNGKLITCPTCHGTGQQRivrgqgffrmvtvttCRTCGGRGripEEKCPRCNG 213
 
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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