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Conserved domains on  [gi|1039775047|ref|XP_006506172|]
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protein SSUH2 homolog isoform X1 [Mus musculus]

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 3.03e-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: 47.25  E-value: 3.03e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039775047 177 CHKCHGRG------RYKCSGCHGAGMVRcsscsgtkrkakQPRRCHLCSGSGRRRCSTCSGRG---NKTCATCKGER 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 3.03e-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: 47.25  E-value: 3.03e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039775047 177 CHKCHGRG------RYKCSGCHGAGMVRcsscsgtkrkakQPRRCHLCSGSGRRRCSTCSGRG---NKTCATCKGER 244
Cdd:cd10719     1 CPTCNGSGakpgtkPKTCPTCGGSGQVR------------QVQGTGFGFFQTQTTCPTCGGTGkiiKDPCPKCKGKG 65
PRK14280 PRK14280
molecular chaperone DnaJ;
176-236 1.42e-06

molecular chaperone DnaJ;


Pssm-ID: 237656 [Multi-domain]  Cd Length: 376  Bit Score: 49.72  E-value: 1.42e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039775047 176 ECHKCHGRG------RYKCSGCHGAGMVRCSSCSGTKRKAKQpRRCHLCSGSGR---RRCSTCSGRGNKT 236
Cdd:PRK14280  145 TCDTCHGSGakpgtsKETCSHCGGSGQVSVEQNTPFGRVVNR-QTCPHCNGTGQeikEKCPTCHGKGKVR 213
DnaJ_CXXCXGXG pfam00684
DnaJ central domain; The central cysteine-rich (CR) domain of DnaJ proteins contains four ...
 177-222 5.05e-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: 43.70  E-value: 5.05e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039775047 177 CHKCHGRG------RYKCSGCHGAGMVR---------------CSSCSGTKRKAKQPrrCHLCSGSG 222
Cdd:pfam00684   1 CPTCNGSGakpgtkPTTCPTCGGTGQVRrvqqtgpgffqmqstCPTCGGTGKIIKDP--CKKCKGKG 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 3.03e-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: 47.25  E-value: 3.03e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039775047 177 CHKCHGRG------RYKCSGCHGAGMVRcsscsgtkrkakQPRRCHLCSGSGRRRCSTCSGRG---NKTCATCKGER 244
Cdd:cd10719     1 CPTCNGSGakpgtkPKTCPTCGGSGQVR------------QVQGTGFGFFQTQTTCPTCGGTGkiiKDPCPKCKGKG 65
PRK14280 PRK14280
molecular chaperone DnaJ;
176-236 1.42e-06

molecular chaperone DnaJ;


Pssm-ID: 237656 [Multi-domain]  Cd Length: 376  Bit Score: 49.72  E-value: 1.42e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039775047 176 ECHKCHGRG------RYKCSGCHGAGMVRCSSCSGTKRKAKQpRRCHLCSGSGR---RRCSTCSGRGNKT 236
Cdd:PRK14280  145 TCDTCHGSGakpgtsKETCSHCGGSGQVSVEQNTPFGRVVNR-QTCPHCNGTGQeikEKCPTCHGKGKVR 213
PRK14293 PRK14293
molecular chaperone DnaJ;
139-235 1.71e-06

molecular chaperone DnaJ;


Pssm-ID: 237663 [Multi-domain]  Cd Length: 374  Bit Score: 49.60  E-value: 1.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039775047 139 GPQRGTSPRLwDMKVQvppmFQE----DTRKLQVPHsslVKECHKCHGRGRYKcsgchGAGMVRCSSCSGtkrkAKQPRR 214
Cdd:PRK14293  112 GPQRGDDLRY-DLKLD----FREaifgGEKEIRIPH---LETCETCRGSGAKP-----GTGPTTCSTCGG----AGQVRR 174

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1039775047 215 --------------CHLCSGSGR---RRCSTCSGRGNK 235
Cdd:PRK14293  175 atrtpfgsftqvseCPTCNGTGQvieDPCDACGGQGVK 212
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
 198-245 2.04e-06

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 49.08  E-value: 2.04e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039775047 198 RCSSCSGTKRK-AKQPRRCHLCSGSGRRR---------------CSTCSGRGN---KTCATCKGERK 245
Cdd:PRK14298  143 RCSTCSGTGAKpGTSPKRCPTCGGTGQVTttrstplgqfvttttCSTCHGRGQvieSPCPVCSGTGK 209
PRK14287 PRK14287
chaperone protein DnaJ; Provisional
 158-233 3.07e-06

chaperone protein DnaJ; Provisional


Pssm-ID: 237659 [Multi-domain]  Cd Length: 371  Bit Score: 48.85  E-value: 3.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039775047 158 MFQEDTrKLQVPHSslvKECHKCHGRGRY------KCSGCHGAGMVRCSSCSGTKRKAKQpRRCHLCSGSG---RRRCST 228
Cdd:PRK14287  126 VFGKET-EIEIPRE---ETCGTCHGSGAKpgtkpeTCSHCGGSGQLNVEQNTPFGRVVNR-RVCHHCEGTGkiiKQKCAT 200


                  ....*
gi 1039775047 229 CSGRG 233
Cdd:PRK14287  201 CGGKG 205
PRK14282 PRK14282
chaperone protein DnaJ; Provisional
 175-225 3.52e-06

chaperone protein DnaJ; Provisional


Pssm-ID: 184603 [Multi-domain]  Cd Length: 369  Bit Score: 48.64  E-value: 3.52e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039775047 175 KECHKCHGRG------RYKCSGCHGAGMVR---------------CSSCSGTKRKAKQprRCHLCSGSGRRR 225
Cdd:PRK14282  153 ETCPHCGGTGvepgsgYVTCPKCHGTGRIReerrsffgvfvsertCERCGGTGKIPGE--YCHECGGSGRIR 222
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
 139-225 4.54e-06

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 48.31  E-value: 4.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039775047 139 GPQRGTSPRlWDMKVQVPPMFQEDTRKLQVPHSslvKECHKCHGRG------RYKCSGCHGAGMVR-------------- 198
Cdd:PRK14298  110 GPRRGSDLR-YDLYITLEEAAFGVRKDIDVPRA---ERCSTCSGTGakpgtsPKRCPTCGGTGQVTttrstplgqfvttt 185

                          90       100
                  ....*....|....*....|....*...
gi 1039775047 199 -CSSCSGTKRKAKQPrrCHLCSGSGRRR 225
Cdd:PRK14298  186 tCSTCHGRGQVIESP--CPVCSGTGKVR 211
DnaJ_CXXCXGXG pfam00684
DnaJ central domain; The central cysteine-rich (CR) domain of DnaJ proteins contains four ...
 177-222 5.05e-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: 43.70  E-value: 5.05e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039775047 177 CHKCHGRG------RYKCSGCHGAGMVR---------------CSSCSGTKRKAKQPrrCHLCSGSG 222
Cdd:pfam00684   1 CPTCNGSGakpgtkPTTCPTCGGTGQVRrvqqtgpgffqmqstCPTCGGTGKIIKDP--CKKCKGKG 65
PLN03165 PLN03165
chaperone protein dnaJ-related; Provisional
 177-233 7.48e-06

chaperone protein dnaJ-related; Provisional


Pssm-ID: 178709 [Multi-domain]  Cd Length: 111  Bit Score: 44.42  E-value: 7.48e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039775047 177 CHKCHGRGRYKCSGCHGAGMVRCSSCSGTKRKAKqprrCHLCSGSGRRRCSTCSGRG 233
Cdd:PLN03165   44 CFPCSGTGAQVCRFCVGSGNVTVELGGGEKEVSK----CINCDGAGSLTCTTCQGSG 96
PRK14276 PRK14276
chaperone protein DnaJ; Provisional
 176-223 3.09e-05

chaperone protein DnaJ; Provisional


Pssm-ID: 237653 [Multi-domain]  Cd Length: 380  Bit Score: 45.46  E-value: 3.09e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039775047 176 ECHKCHGRGRYK------CSGCHGA-----------GMVR----CSSCSGTKRKAKQPrrCHLCSGSGR 223
Cdd:PRK14276  148 TCHTCNGSGAKPgtspvtCGKCHGSgvitvdtqtplGMMRrqvtCDVCHGTGKEIKEP--CQTCHGTGH 214
PRK14295 PRK14295
molecular chaperone DnaJ;
199-242 4.78e-05

molecular chaperone DnaJ;


Pssm-ID: 237665 [Multi-domain]  Cd Length: 389  Bit Score: 44.84  E-value: 4.78e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039775047 199 CSSCSGTKRKA-KQPRRCHLCSGSGRRR-----------CSTCSGRG---NKTCATCKG 242
Cdd:PRK14295  169 CPACSGTGAKNgTTPRVCPTCSGTGQVSrnsggfslsepCPDCKGRGliaDDPCLVCKG 227
DnaJ_C pfam01556
DnaJ C terminal domain; This family consists of the C terminal region of the DnaJ protein. It ...
 163-228 7.45e-05

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: 43.40  E-value: 7.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039775047 163 TRKLQVPHsslVKECHKCHGRG------RYKCSGCHGAGMVR-----------CSSCSGTKRKAKQPRRChlCSGSGRRR 225
Cdd:pfam01556  17 TKKIKITR---NVICDTCGGSGakpgtsPKTCPCCGGGGQVRrqfgffstctcCPCCGGGGKIIDKCCKC--CGGGGVVE 91


                  ...
gi 1039775047 226 CST 228
Cdd:pfam01556  92 KKT 94
PRK14285 PRK14285
chaperone protein DnaJ; Provisional
 199-248 1.42e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 172773 [Multi-domain]  Cd Length: 365  Bit Score: 43.44  E-value: 1.42e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039775047 199 CSSCSGTK-RKAKQPRRCHLCSGSGR-----------RRCSTCSGRG---NKTCATCKGERKLEH 248
Cdd:PRK14285  149 CESCLGKKsEKGTSPSICNMCNGSGRvmqgggffrvtTTCPKCYGNGkiiSNPCKSCKGKGSLKK 213
DnaJ_zf cd10719
Zinc finger domain of DnaJ and HSP40; Central/middle or CxxCxGxG-motif containing domain of ...
 199-245 2.47e-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: 2.47e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039775047 199 CSSCSGTKRKA-KQPRRCHLCSGSGRRRCSTCSGRGN----KTCATCKGERK 245
Cdd:cd10719     1 CPTCNGSGAKPgTKPKTCPTCGGSGQVRQVQGTGFGFfqtqTTCPTCGGTGK 52
PRK14296 PRK14296
chaperone protein DnaJ; Provisional
 173-233 2.83e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 237666 [Multi-domain]  Cd Length: 372  Bit Score: 42.63  E-value: 2.83e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039775047 173 LVKECHKCHGRGRYK------CSGCHGAGMVRCSSCSGTkRKAKQPRRCHLCSGSG---RRRCSTCSGRG 233
Cdd:PRK14296  148 LLTNCSKCFGSGAESnsdihiCNNCHGTGEVLVQKNMGF-FQFQQSAKCNVCNGAGkiiKNKCKNCKGKG 216
PLN03165 PLN03165
chaperone protein dnaJ-related; Provisional
 206-245 6.68e-04

chaperone protein dnaJ-related; Provisional


Pssm-ID: 178709 [Multi-domain]  Cd Length: 111  Bit Score: 39.03  E-value: 6.68e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1039775047 206 KRKAKQPrrCHLCSGSGRRRCSTCSGRGNKTCATCKGERK 245
Cdd:PLN03165   37 KRENTQP--CFPCSGTGAQVCRFCVGSGNVTVELGGGEKE 74
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 177-198 7.00e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 41.28  E-value: 7.00e-04
                          10        20
                  ....*....|....*....|....*
gi 1039775047 177 CHKCHGRGRY---KCSGCHGAGMVR 198
Cdd:PRK10767  184 CPTCHGRGKIikdPCKKCHGQGRVE 208
PRK14277 PRK14277
chaperone protein DnaJ; Provisional
 199-246 1.43e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 184599 [Multi-domain]  Cd Length: 386  Bit Score: 40.17  E-value: 1.43e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1039775047 199 CSSCSGTKRK-AKQPRRCHLCSGSG--RRRCSTCSGR--GNKTCATCKGERKL 246
Cdd:PRK14277  158 CDVCKGSGAKpGSKPVTCPVCHGTGqvRTRQNTPFGRivNIRTCDRCHGEGKI 210
DnaJ_CXXCXGXG pfam00684
DnaJ central domain; The central cysteine-rich (CR) domain of DnaJ proteins contains four ...
 174-206 1.73e-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: 36.38  E-value: 1.73e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1039775047 174 VKECHKCHGRGRYK---------------CSGCHGAGMV---RCSSCSGTK 206
Cdd:pfam00684  15 PTTCPTCGGTGQVRrvqqtgpgffqmqstCPTCGGTGKIikdPCKKCKGKG 65
DnaJ_CXXCXGXG pfam00684
DnaJ central domain; The central cysteine-rich (CR) domain of DnaJ proteins contains four ...
 199-245 1.73e-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: 36.38  E-value: 1.73e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039775047 199 CSSCSGTK-RKAKQPRRCHLCSGSGRRRCSTCSGRGN----KTCATCKGERK 245
Cdd:pfam00684   1 CPTCNGSGaKPGTKPTTCPTCGGTGQVRRVQQTGPGFfqmqSTCPTCGGTGK 52
PRK14290 PRK14290
chaperone protein DnaJ; Provisional
 199-242 1.89e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 172778 [Multi-domain]  Cd Length: 365  Bit Score: 39.91  E-value: 1.89e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039775047 199 CSSCSGTKRKAKQPRRCHLCSGSGRRR---------------CSTCSGRG---NKTCATCKG 242
Cdd:PRK14290  152 CPDCSGTGAKNGKLITCPTCHGTGQQRivrgqgffrmvtvttCRTCGGRGripEEKCPRCNG 213
DnaJ_C pfam01556
DnaJ C terminal domain; This family consists of the C terminal region of the DnaJ protein. It ...
 196-247 3.01e-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: 38.77  E-value: 3.01e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039775047 196 MVRCSSCSGTK-RKAKQPRRCHLCSGSGRRR--------CSTCSGRG------NKTCATCKGERKLE 247
Cdd:pfam01556  25 NVICDTCGGSGaKPGTSPKTCPCCGGGGQVRrqfgffstCTCCPCCGgggkiiDKCCKCCGGGGVVE 91
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 196-243 3.68e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 38.97  E-value: 3.68e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039775047 196 MVRCSSCSGTKRKAkqprrchlcsGSGRRRCSTCSGRGN-----------KTCATCKGE 243
Cdd:PRK10767  142 LVTCDTCHGSGAKP----------GTSPKTCPTCHGAGQvrmqqgfftvqQTCPTCHGR 190
DnaJ_zf cd10719
Zinc finger domain of DnaJ and HSP40; Central/middle or CxxCxGxG-motif containing domain of ...
 169-222 4.20e-03

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: 35.31  E-value: 4.20e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039775047 169 PHSSLVKECHKCHGRGRYKCSGCHGAGMVR----CSSCSGTKRKAKQPrrCHLCSGSG 222
Cdd:cd10719    10 KPGTKPKTCPTCGGSGQVRQVQGTGFGFFQtqttCPTCGGTGKIIKDP--CPKCKGKG 65
PRK14291 PRK14291
chaperone protein DnaJ; Provisional
 197-243 5.50e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 237661 [Multi-domain]  Cd Length: 382  Bit Score: 38.60  E-value: 5.50e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039775047 197 VRCSSCSGTKRKAkqprrchlcsGSGRRRCSTCSGRGN-----------KTCATCKGE 243
Cdd:PRK14291  157 VPCEACGGTGYDP----------GSGEKVCPTCGGSGEiyqrggffrisQTCPTCGGE 204
GRX_GRX_like cd03031
Glutaredoxin (GRX) family, GRX-like domain containing protein subfamily; composed of ...
 173-229 7.89e-03

Glutaredoxin (GRX) family, GRX-like domain containing protein subfamily; composed of uncharacterized eukaryotic proteins containing a GRX-like domain having only one conserved cysteine, aligning to the C-terminal cysteine of the CXXC motif of GRXs. This subfamily is predominantly composed of plant proteins. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins via a redox active CXXC motif using a similar dithiol mechanism employed by TRXs. GRX has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. Proteins containing only the C-terminal cysteine are generally redox inactive.


Pssm-ID: 239329 [Multi-domain]  Cd Length: 147  Bit Score: 36.45  E-value: 7.89e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039775047 173 LVKECHKChgRGRYKCSGCHGAGMVRCSSCSGTKRKAKQprrcHLCSGSGRRRCSTC 229
Cdd:cd03031    89 LLKGIRAR--AGGGVCEGCGGARFVPCSECNGSCKVFAE----NATAAGGFLRCPEC 139
 
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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