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Conserved domains on  [gi|1376953209|ref|XP_002980587|]
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protein SSUH2 homolog [Selaginella moellendorffii]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK14291 super family cl36359
chaperone protein DnaJ; Provisional
 236-304 1.97e-05

chaperone protein DnaJ; Provisional


The actual alignment was detected with superfamily member PRK14291:

Pssm-ID: 237661 [Multi-domain]  Cd Length: 382  Bit Score: 46.69  E-value: 1.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376953209 236 NLQQRKKFTCSRCNGRGLIAhldGSDS-SCKECKGSGKVY-----------CPRCHSRGLL--ACEHCKSAGSFVSSMSV 301
Cdd:PRK14291  150 SLEVPRYVPCEACGGTGYDP---GSGEkVCPTCGGSGEIYqrggffrisqtCPTCGGEGVLrePCSKCNGRGLVIKKETI 226


                  ...
gi 1376953209 302 RVK 304
Cdd:PRK14291  227 KVR 229
PRK14298 super family cl32989
chaperone protein DnaJ; Provisional
 194-273 1.33e-03

chaperone protein DnaJ; Provisional


The actual alignment was detected with superfamily member PRK14298:

Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 40.60  E-value: 1.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376953209 194 LFVSSKEAL------IKVPHSESVEQCTGCLGQGDIACHVCTIYDDSGNLQQRK-----KF----TCSRCNGRGLIAhld 258
Cdd:PRK14298  121 LYITLEEAAfgvrkdIDVPRAERCSTCSGTGAKPGTSPKRCPTCGGTGQVTTTRstplgQFvtttTCSTCHGRGQVI--- 197

                          90
                  ....*....|....*
gi 1376953209 259 gsDSSCKECKGSGKV 273
Cdd:PRK14298  198 --ESPCPVCSGTGKV 210
 
Name Accession Description Interval E-value
PRK14291 PRK14291
chaperone protein DnaJ; Provisional
 236-304 1.97e-05

chaperone protein DnaJ; Provisional


Pssm-ID: 237661 [Multi-domain]  Cd Length: 382  Bit Score: 46.69  E-value: 1.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376953209 236 NLQQRKKFTCSRCNGRGLIAhldGSDS-SCKECKGSGKVY-----------CPRCHSRGLL--ACEHCKSAGSFVSSMSV 301
Cdd:PRK14291  150 SLEVPRYVPCEACGGTGYDP---GSGEkVCPTCGGSGEIYqrggffrisqtCPTCGGEGVLrePCSKCNGRGLVIKKETI 226


                  ...
gi 1376953209 302 RVK 304
Cdd:PRK14291  227 KVR 229
DnaJ_zf cd10719
Zinc finger domain of DnaJ and HSP40; Central/middle or CxxCxGxG-motif containing domain of ...
 225-282 1.58e-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: 39.55  E-value: 1.58e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1376953209 225 CHVCtiyDDSGNLQQRKKFTCSRCNGRGLIAHLDGSD-------SSCKECKGSGKVY---CPRCHSRG 282
Cdd:cd10719     1 CPTC---NGSGAKPGTKPKTCPTCGGSGQVRQVQGTGfgffqtqTTCPTCGGTGKIIkdpCPKCKGKG 65
DnaJ_CXXCXGXG pfam00684
DnaJ central domain; The central cysteine-rich (CR) domain of DnaJ proteins contains four ...
 245-293 1.32e-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: 37.15  E-value: 1.32e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1376953209 245 CSRCNGRGliAHLDGSDSSCKECKGSGKVY---------------CPRCHSRGLL---ACEHCKSAG 293
Cdd:pfam00684   1 CPTCNGSG--AKPGTKPTTCPTCGGTGQVRrvqqtgpgffqmqstCPTCGGTGKIikdPCKKCKGKG 65
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
 194-273 1.33e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 40.60  E-value: 1.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376953209 194 LFVSSKEAL------IKVPHSESVEQCTGCLGQGDIACHVCTIYDDSGNLQQRK-----KF----TCSRCNGRGLIAhld 258
Cdd:PRK14298  121 LYITLEEAAfgvrkdIDVPRAERCSTCSGTGAKPGTSPKRCPTCGGTGQVTTTRstplgQFvtttTCSTCHGRGQVI--- 197

                          90
                  ....*....|....*
gi 1376953209 259 gsDSSCKECKGSGKV 273
Cdd:PRK14298  198 --ESPCPVCSGTGKV 210
 
Name Accession Description Interval E-value
PRK14291 PRK14291
chaperone protein DnaJ; Provisional
 236-304 1.97e-05

chaperone protein DnaJ; Provisional


Pssm-ID: 237661 [Multi-domain]  Cd Length: 382  Bit Score: 46.69  E-value: 1.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376953209 236 NLQQRKKFTCSRCNGRGLIAhldGSDS-SCKECKGSGKVY-----------CPRCHSRGLL--ACEHCKSAGSFVSSMSV 301
Cdd:PRK14291  150 SLEVPRYVPCEACGGTGYDP---GSGEkVCPTCGGSGEIYqrggffrisqtCPTCGGEGVLrePCSKCNGRGLVIKKETI 226


                  ...
gi 1376953209 302 RVK 304
Cdd:PRK14291  227 KVR 229
DnaJ_zf cd10719
Zinc finger domain of DnaJ and HSP40; Central/middle or CxxCxGxG-motif containing domain of ...
 225-282 1.58e-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: 39.55  E-value: 1.58e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1376953209 225 CHVCtiyDDSGNLQQRKKFTCSRCNGRGLIAHLDGSD-------SSCKECKGSGKVY---CPRCHSRG 282
Cdd:cd10719     1 CPTC---NGSGAKPGTKPKTCPTCGGSGQVRQVQGTGfgffqtqTTCPTCGGTGKIIkdpCPKCKGKG 65
PRK14280 PRK14280
molecular chaperone DnaJ;
196-282 1.70e-04

molecular chaperone DnaJ;


Pssm-ID: 237656 [Multi-domain]  Cd Length: 376  Bit Score: 43.56  E-value: 1.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376953209 196 VSSKEALIKVPHSESVEQCTGclgqgdiachvctiyddSGNLQQRKKFTCSRCNGRGLIAHLDG-------SDSSCKECK 268
Cdd:PRK14280  131 VFGKEKEIEIPKEETCDTCHG-----------------SGAKPGTSKETCSHCGGSGQVSVEQNtpfgrvvNRQTCPHCN 193

                          90
                  ....*....|....*..
gi 1376953209 269 GSGKVY---CPRCHSRG 282
Cdd:PRK14280  194 GTGQEIkekCPTCHGKG 210
DnaJ_zf cd10719
Zinc finger domain of DnaJ and HSP40; Central/middle or CxxCxGxG-motif containing domain of ...
 206-271 2.32e-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: 39.16  E-value: 2.32e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1376953209 206 PHSESVEQCTGCLGQGdiachVCTIYDDSGNLQQRKKFTCSRCNGRGLIAhldgsDSSCKECKGSG 271
Cdd:cd10719    10 KPGTKPKTCPTCGGSG-----QVRQVQGTGFGFFQTQTTCPTCGGTGKII-----KDPCPKCKGKG 65
PRK14301 PRK14301
chaperone protein DnaJ; Provisional
 237-303 2.33e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 237668 [Multi-domain]  Cd Length: 373  Bit Score: 43.19  E-value: 2.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376953209 237 LQQRKKFTCSRCNGRGliAHLDGSDSSCKECKGSGKVY-----------CPRCHSRGLL---ACEHCKSAGSF--VSSMS 300
Cdd:PRK14301  139 LRIPKNVTCDDCGGSG--AAPGTSPETCRHCGGSGQVRqsqgffqiavpCPVCRGEGRVithPCPKCKGSGIVqqTRELK 216


                  ...
gi 1376953209 301 VRV 303
Cdd:PRK14301  217 VRI 219
PRK14284 PRK14284
chaperone protein DnaJ; Provisional
 244-303 2.49e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 237658 [Multi-domain]  Cd Length: 391  Bit Score: 42.91  E-value: 2.49e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1376953209 244 TCSRCNGRGliAHLDGSDSSCKECKGSGKVY-----------CPRCHSRGLL---ACEHCKSAGSFVSSMSVRV 303
Cdd:PRK14284  160 SCDACSGSG--ANSSQGIKVCDRCKGSGQVVqsrgffsmastCPECGGEGRVitdPCSVCRGQGRIKDKRSVHV 231
PRK14286 PRK14286
chaperone protein DnaJ; Provisional
 244-293 3.43e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 172774 [Multi-domain]  Cd Length: 372  Bit Score: 42.67  E-value: 3.43e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1376953209 244 TCSRCNGRGliAHLDGSDSSCKECKGSGKV-----------YCPRCHSRGLLACEHCKSAG 293
Cdd:PRK14286  152 SCVDCNGSG--ASKGSSPTTCPDCGGSGQIrrtqgffsvatTCPTCRGKGTVISNPCKTCG 210
PRK14289 PRK14289
molecular chaperone DnaJ;
240-293 3.89e-04

molecular chaperone DnaJ;


Pssm-ID: 237660 [Multi-domain]  Cd Length: 386  Bit Score: 42.51  E-value: 3.89e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1376953209 240 RKKFTCSRCNGRGliAHLDGSDSSCKECKGSGKV---------------YCPRCHSRGLL---ACEHCKSAG 293
Cdd:PRK14289  152 KKYVPCSHCHGTG--AEGNNGSETCPTCKGSGSVtrvqntilgtmqtqsTCPTCNGEGKIikkKCKKCGGEG 221
DnaJ_zf cd10719
Zinc finger domain of DnaJ and HSP40; Central/middle or CxxCxGxG-motif containing domain of ...
 245-293 6.65e-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: 38.01  E-value: 6.65e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1376953209 245 CSRCNGRGliAHLDGSDSSCKECKGSGKVY---------------CPRCHSRGLL---ACEHCKSAG 293
Cdd:cd10719     1 CPTCNGSG--AKPGTKPKTCPTCGGSGQVRqvqgtgfgffqtqttCPTCGGTGKIikdPCPKCKGKG 65
PRK14301 PRK14301
chaperone protein DnaJ; Provisional
 222-284 8.78e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 237668 [Multi-domain]  Cd Length: 373  Bit Score: 41.27  E-value: 8.78e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1376953209 222 DIACHVCtiyDDSGNLQQRKKFTCSRCNGRGLIAHLDG---SDSSCKECKGSGKVY---CPRCHSRGLL 284
Cdd:PRK14301  144 NVTCDDC---GGSGAAPGTSPETCRHCGGSGQVRQSQGffqIAVPCPVCRGEGRVIthpCPKCKGSGIV 209
PRK14294 PRK14294
chaperone protein DnaJ; Provisional
 240-304 1.06e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 237664 [Multi-domain]  Cd Length: 366  Bit Score: 40.90  E-value: 1.06e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1376953209 240 RKKFTCSRCNGRGliAHLDGSDSSCKECKGSGKVY-----------CPRCHSRGLL---ACEHCKSAGSFVSSMSVRVK 304
Cdd:PRK14294  142 QKLETCEECHGSG--CEPGTSPTTCPQCGGSGQVTqsqgffsirttCPRCRGMGKVivsPCKTCHGQGRVRVSKTVQVK 218
DnaJ_CXXCXGXG pfam00684
DnaJ central domain; The central cysteine-rich (CR) domain of DnaJ proteins contains four ...
 245-293 1.32e-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: 37.15  E-value: 1.32e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1376953209 245 CSRCNGRGliAHLDGSDSSCKECKGSGKVY---------------CPRCHSRGLL---ACEHCKSAG 293
Cdd:pfam00684   1 CPTCNGSG--AKPGTKPTTCPTCGGTGQVRrvqqtgpgffqmqstCPTCGGTGKIikdPCKKCKGKG 65
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
 194-273 1.33e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 40.60  E-value: 1.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376953209 194 LFVSSKEAL------IKVPHSESVEQCTGCLGQGDIACHVCTIYDDSGNLQQRK-----KF----TCSRCNGRGLIAhld 258
Cdd:PRK14298  121 LYITLEEAAfgvrkdIDVPRAERCSTCSGTGAKPGTSPKRCPTCGGTGQVTTTRstplgQFvtttTCSTCHGRGQVI--- 197

                          90
                  ....*....|....*
gi 1376953209 259 gsDSSCKECKGSGKV 273
Cdd:PRK14298  198 --ESPCPVCSGTGKV 210
PRK14289 PRK14289
molecular chaperone DnaJ;
208-274 1.35e-03

molecular chaperone DnaJ;


Pssm-ID: 237660 [Multi-domain]  Cd Length: 386  Bit Score: 40.58  E-value: 1.35e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1376953209 208 SESVEQCTGCLGQGDIACHVCTIYddsGNLQQRKkfTCSRCNGRGLIAhldgsDSSCKECKGSGKVY 274
Cdd:PRK14289  168 NNGSETCPTCKGSGSVTRVQNTIL---GTMQTQS--TCPTCNGEGKII-----KKKCKKCGGEGIVY 224
PRK14296 PRK14296
chaperone protein DnaJ; Provisional
 211-272 1.46e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 237666 [Multi-domain]  Cd Length: 372  Bit Score: 40.70  E-value: 1.46e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1376953209 211 VEQCTGCLGQG-----DIacHVCT---------IYDDSGNLQQRKKFTCSRCNGRGLIAhldgsDSSCKECKGSGK 272
Cdd:PRK14296  149 LTNCSKCFGSGaesnsDI--HICNnchgtgevlVQKNMGFFQFQQSAKCNVCNGAGKII-----KNKCKNCKGKGK 217
PRK14284 PRK14284
chaperone protein DnaJ; Provisional
 227-282 6.84e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 237658 [Multi-domain]  Cd Length: 391  Bit Score: 38.67  E-value: 6.84e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1376953209 227 VCTIYDDSGNLQQRKKFTCSRCNGRGLIAHLDG---SDSSCKECKGSGKVY---CPRCHSRG 282
Cdd:PRK14284  160 SCDACSGSGANSSQGIKVCDRCKGSGQVVQSRGffsMASTCPECGGEGRVItdpCSVCRGQG 221
DnaJ_CXXCXGXG pfam00684
DnaJ central domain; The central cysteine-rich (CR) domain of DnaJ proteins contains four ...
 225-282 7.26e-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: 34.84  E-value: 7.26e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1376953209 225 CHVCtiyDDSGNLQQRKKFTCSRCNGRGLIAHLDGSD-------SSCKECKGSGKVY---CPRCHSRG 282
Cdd:pfam00684   1 CPTC---NGSGAKPGTKPTTCPTCGGTGQVRRVQQTGpgffqmqSTCPTCGGTGKIIkdpCKKCKGKG 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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