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Conserved domains on  [gi|186511163|ref|NP_191361|]
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Chaperone DnaJ-domain superfamily protein [Arabidopsis thaliana]

Protein Classification

J domain-containing protein( domain architecture ID 10644999)

J domain-containing protein similar to molecular chaperone DnaJ, a protein that plays crucial roles in protein translation, folding, unfolding, translocation, and degradation, primarily by stimulating the ATPase activity of Hsp70

CATH:  1.10.287.110
Gene Ontology:  GO:0006457
PubMed:  35729039|9644977|8016869|15170475
SCOP:  4000605

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DnaJ smart00271
DnaJ molecular chaperone homology domain;
190-250 4.40e-11

DnaJ molecular chaperone homology domain;


:

Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 56.86  E-value: 4.40e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 186511163   190 ESHRQTLGLSSSgpLNLEDVKIAYRACALKWHPDRhHTSTKNEAEEKFKLCTVAYQSLCEK 250
Cdd:smart00271   1 TDYYEILGVPRD--ASLDEIKKAYRKLALKYHPDK-NPGDKEEAEEKFKEINEAYEVLSDP 58
 
Name Accession Description Interval E-value
DnaJ smart00271
DnaJ molecular chaperone homology domain;
190-250 4.40e-11

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 56.86  E-value: 4.40e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 186511163   190 ESHRQTLGLSSSgpLNLEDVKIAYRACALKWHPDRhHTSTKNEAEEKFKLCTVAYQSLCEK 250
Cdd:smart00271   1 TDYYEILGVPRD--ASLDEIKKAYRKLALKYHPDK-NPGDKEEAEEKFKEINEAYEVLSDP 58
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 194-248 2.48e-08

DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is thought that this domain mediates the interaction. DnaJ-domain is therefore part of a chaperone (protein folding) system. The T-antigens, although not in Prosite are confirmed as DnaJ containing domains from literature.


Pssm-ID: 395170 [Multi-domain]  Cd Length: 63  Bit Score: 49.39  E-value: 2.48e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 186511163  194 QTLGLSSSgpLNLEDVKIAYRACALKWHPDRHhtSTKNEAEEKFKLCTVAYQSLC 248
Cdd:pfam00226   4 EILGVSPD--ASDEEIKKAYRKLALKYHPDKN--PGDPEAEEKFKEINEAYEVLS 54
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 191-247 3.19e-08

DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440252 [Multi-domain]  Cd Length: 139  Bit Score: 51.24  E-value: 3.19e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 186511163 191 SHRQTLGLSSSGPLnlEDVKIAYRACALKWHPDRHHTSTknEAEEKFKLCTVAYQSL 247
Cdd:COG0484    1 DYYEILGVSRDASA--EEIKKAYRKLAKKYHPDRNPGDP--EAEEKFKEINEAYEVL 53
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
 194-247 5.46e-08

chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the DnaK-DnaJ-GrpE chaperone system. The three components typically are encoded by consecutive genes. DnaJ homologs occur in many genomes, typically not near DnaK and GrpE-like genes; most such genes are not included by this family. Eukaryotic (mitochondrial and chloroplast) forms are not included in the scope of this family.


Pssm-ID: 274090 [Multi-domain]  Cd Length: 354  Bit Score: 52.60  E-value: 5.46e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 186511163  194 QTLGLSSSGplNLEDVKIAYRACALKWHPDRHhtstKN-EAEEKFKLCTVAYQSL 247
Cdd:TIGR02349   4 EILGVSKDA--SEEEIKKAYRKLAKKYHPDRN----KDkEAEEKFKEINEAYEVL 52
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 192-248 1.46e-07

DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) 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 chaperonine family. Hsp40 proteins are characterized by the presence of a J domain, which mediates the interaction with Hsp70. They may contain other domains as well, and the architectures provide a means of classification.


Pssm-ID: 99751 [Multi-domain]  Cd Length: 55  Bit Score: 47.15  E-value: 1.46e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 186511163 192 HRQTLGLSSSgpLNLEDVKIAYRACALKWHPDRHhtSTKNEAEEKFKLCTVAYQSLC 248
Cdd:cd06257    2 YYDILGVPPD--ASDEEIKKAYRKLALKYHPDKN--PDDPEAEEKFKEINEAYEVLS 54
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 207-247 1.66e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 51.30  E-value: 1.66e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 186511163 207 EDVKIAYRACALKWHPDRHHTSTknEAEEKFKLCTVAYQSL 247
Cdd:PRK10767  19 DEIKKAYRKLAMKYHPDRNPGDK--EAEEKFKEIKEAYEVL 57
 
Name Accession Description Interval E-value
DnaJ smart00271
DnaJ molecular chaperone homology domain;
190-250 4.40e-11

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 56.86  E-value: 4.40e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 186511163   190 ESHRQTLGLSSSgpLNLEDVKIAYRACALKWHPDRhHTSTKNEAEEKFKLCTVAYQSLCEK 250
Cdd:smart00271   1 TDYYEILGVPRD--ASLDEIKKAYRKLALKYHPDK-NPGDKEEAEEKFKEINEAYEVLSDP 58
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 194-248 2.48e-08

DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is thought that this domain mediates the interaction. DnaJ-domain is therefore part of a chaperone (protein folding) system. The T-antigens, although not in Prosite are confirmed as DnaJ containing domains from literature.


Pssm-ID: 395170 [Multi-domain]  Cd Length: 63  Bit Score: 49.39  E-value: 2.48e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 186511163  194 QTLGLSSSgpLNLEDVKIAYRACALKWHPDRHhtSTKNEAEEKFKLCTVAYQSLC 248
Cdd:pfam00226   4 EILGVSPD--ASDEEIKKAYRKLALKYHPDKN--PGDPEAEEKFKEINEAYEVLS 54
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 191-247 3.19e-08

DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440252 [Multi-domain]  Cd Length: 139  Bit Score: 51.24  E-value: 3.19e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 186511163 191 SHRQTLGLSSSGPLnlEDVKIAYRACALKWHPDRHHTSTknEAEEKFKLCTVAYQSL 247
Cdd:COG0484    1 DYYEILGVSRDASA--EEIKKAYRKLAKKYHPDRNPGDP--EAEEKFKEINEAYEVL 53
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
 194-247 5.46e-08

chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the DnaK-DnaJ-GrpE chaperone system. The three components typically are encoded by consecutive genes. DnaJ homologs occur in many genomes, typically not near DnaK and GrpE-like genes; most such genes are not included by this family. Eukaryotic (mitochondrial and chloroplast) forms are not included in the scope of this family.


Pssm-ID: 274090 [Multi-domain]  Cd Length: 354  Bit Score: 52.60  E-value: 5.46e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 186511163  194 QTLGLSSSGplNLEDVKIAYRACALKWHPDRHhtstKN-EAEEKFKLCTVAYQSL 247
Cdd:TIGR02349   4 EILGVSKDA--SEEEIKKAYRKLAKKYHPDRN----KDkEAEEKFKEINEAYEVL 52
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 192-248 1.46e-07

DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) 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 chaperonine family. Hsp40 proteins are characterized by the presence of a J domain, which mediates the interaction with Hsp70. They may contain other domains as well, and the architectures provide a means of classification.


Pssm-ID: 99751 [Multi-domain]  Cd Length: 55  Bit Score: 47.15  E-value: 1.46e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 186511163 192 HRQTLGLSSSgpLNLEDVKIAYRACALKWHPDRHhtSTKNEAEEKFKLCTVAYQSLC 248
Cdd:cd06257    2 YYDILGVPPD--ASDEEIKKAYRKLALKYHPDKN--PDDPEAEEKFKEINEAYEVLS 54
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 207-247 1.66e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 51.30  E-value: 1.66e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 186511163 207 EDVKIAYRACALKWHPDRHHTSTknEAEEKFKLCTVAYQSL 247
Cdd:PRK10767  19 DEIKKAYRKLAMKYHPDRNPGDK--EAEEKFKEIKEAYEVL 57
PRK14282 PRK14282
chaperone protein DnaJ; Provisional
 207-253 2.76e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 184603 [Multi-domain]  Cd Length: 369  Bit Score: 50.56  E-value: 2.76e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 186511163 207 EDVKIAYRACALKWHPDRHHTSTKnEAEEKFKLCTVAYQSLC--EKLAM 253
Cdd:PRK14282  19 EEIKRAYKRLVKEWHPDRHPENRK-EAEQKFKEIQEAYEVLSdpQKRAM 66
PRK14286 PRK14286
chaperone protein DnaJ; Provisional
 188-247 3.90e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 172774 [Multi-domain]  Cd Length: 372  Bit Score: 50.37  E-value: 3.90e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511163 188 NQESHRQTLGLSSSGplNLEDVKIAYRACALKWHPDRHHTStkNEAEEKFKLCTVAYQSL 247
Cdd:PRK14286   2 SERSYYDILGVSKSA--NDEEIKSAYRKLAIKYHPDKNKGN--KESEEKFKEATEAYEIL 57
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
187-248 4.34e-07

Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 46.63  E-value: 4.34e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 186511163 187 PNQESHRQTLGLSSSGPLnlEDVKIAYRACALKWHPDRhHTSTKNEAEEKFKLCTVAYQSLC 248
Cdd:COG2214    2 PDLKDHYAVLGVPPDASL--EEIRQAYRRLAKLLHPDR-GGELKALAEELFQRLNEAYEVLS 60
PRK14290 PRK14290
chaperone protein DnaJ; Provisional
 207-249 2.55e-06

chaperone protein DnaJ; Provisional


Pssm-ID: 172778 [Multi-domain]  Cd Length: 365  Bit Score: 47.62  E-value: 2.55e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 186511163 207 EDVKIAYRACALKWHPDRhHTSTKNEAEEKFKLCTVAYQSLCE 249
Cdd:PRK14290  18 EDIKKAFRELAKKWHPDL-HPGNKAEAEEKFKEISEAYEVLSD 59
PRK14297 PRK14297
molecular chaperone DnaJ;
207-247 3.74e-06

molecular chaperone DnaJ;


Pssm-ID: 184611 [Multi-domain]  Cd Length: 380  Bit Score: 47.47  E-value: 3.74e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 186511163 207 EDVKIAYRACALKWHPDRHHTSTknEAEEKFKLCTVAYQSL 247
Cdd:PRK14297  19 DEIKKAFRKLAIKYHPDKNKGNK--EAEEKFKEINEAYQVL 57
SEC63 COG5407
Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular ...
 194-247 4.95e-06

Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 444165 [Multi-domain]  Cd Length: 61  Bit Score: 43.06  E-value: 4.95e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 186511163 194 QTLGLSSSGPLnlEDVKIAYRACALKWHPDRHHTSTKneAEEKFKLCTVAYQSL 247
Cdd:COG5407    4 EVLGVAKTASA--DEIKKAYRKLAKKYHPDRNKGDPK--AEERFKEINEAYELL 53
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
 196-247 6.67e-06

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 46.38  E-value: 6.67e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 186511163 196 LGLSSSGplNLEDVKIAYRACALKWHPDRhhtSTKNEAEEKFKLCTVAYQSL 247
Cdd:PRK14298  11 LGLSKDA--SVEDIKKAYRKLAMKYHPDK---NKEPDAEEKFKEISEAYAVL 57
PRK14281 PRK14281
chaperone protein DnaJ; Provisional
 194-247 1.89e-05

chaperone protein DnaJ; Provisional


Pssm-ID: 237657 [Multi-domain]  Cd Length: 397  Bit Score: 45.18  E-value: 1.89e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 186511163 194 QTLGLSSSGplNLEDVKIAYRACALKWHPDRHhtSTKNEAEEKFKLCTVAYQSL 247
Cdd:PRK14281   7 EVLGVSRSA--DKDEIKKAYRKLALKYHPDKN--PDNKEAEEHFKEVNEAYEVL 56
PRK14291 PRK14291
chaperone protein DnaJ; Provisional
 207-247 3.86e-05

chaperone protein DnaJ; Provisional


Pssm-ID: 237661 [Multi-domain]  Cd Length: 382  Bit Score: 44.38  E-value: 3.86e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 186511163 207 EDVKIAYRACALKWHPDrhhTSTKNEAEEKFKLCTVAYQSL 247
Cdd:PRK14291  18 EEIKKAYRRLARKYHPD---FNKNPEAEEKFKEINEAYQVL 55
PRK14294 PRK14294
chaperone protein DnaJ; Provisional
 207-249 4.62e-05

chaperone protein DnaJ; Provisional


Pssm-ID: 237664 [Multi-domain]  Cd Length: 366  Bit Score: 43.98  E-value: 4.62e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 186511163 207 EDVKIAYRACALKWHPDRHhtSTKNEAEEKFKLCTVAYQSLCE 249
Cdd:PRK14294  19 EEIKKSYRKLAMKYHPDRN--PGDKEAEELFKEAAEAYEVLSD 59
PRK10266 PRK10266
curved DNA-binding protein;
205-247 1.17e-04

curved DNA-binding protein;


Pssm-ID: 182347 [Multi-domain]  Cd Length: 306  Bit Score: 42.50  E-value: 1.17e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 186511163 205 NLEDVKIAYRACALKWHPDrhhTSTKNEAEEKFKLCTVAYQSL 247
Cdd:PRK10266  17 DLKTIKTAYRRLARKYHPD---VSKEPDAEARFKEVAEAWEVL 56
PRK14301 PRK14301
chaperone protein DnaJ; Provisional
 207-247 2.15e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 237668 [Multi-domain]  Cd Length: 373  Bit Score: 42.04  E-value: 2.15e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 186511163 207 EDVKIAYRACALKWHPDRHHTSTknEAEEKFKLCTVAYQSL 247
Cdd:PRK14301  19 DEIKKAYRKLALQYHPDRNPDNP--EAEQKFKEAAEAYEVL 57
PRK14292 PRK14292
chaperone protein DnaJ; Provisional
 196-247 3.13e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 237662 [Multi-domain]  Cd Length: 371  Bit Score: 41.41  E-value: 3.13e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 186511163 196 LGLSSSGplNLEDVKIAYRACALKWHPDRHHTSTkneAEEKFKLCTVAYQSL 247
Cdd:PRK14292   8 LGVSRTA--SADEIKSAYRKLALKYHPDRNKEKG---AAEKFAQINEAYAVL 54
PRK14283 PRK14283
chaperone protein DnaJ; Provisional
 207-247 3.34e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 184604 [Multi-domain]  Cd Length: 378  Bit Score: 41.35  E-value: 3.34e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 186511163 207 EDVKIAYRACALKWHPDrhhTSTKNEAEEKFKLCTVAYQSL 247
Cdd:PRK14283  20 KEIKKAYRKLARKYHPD---VSEEEGAEEKFKEISEAYAVL 57
PRK14288 PRK14288
molecular chaperone DnaJ;
205-250 3.48e-04

molecular chaperone DnaJ;


Pssm-ID: 172776 [Multi-domain]  Cd Length: 369  Bit Score: 41.21  E-value: 3.48e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 186511163 205 NLEDVKIAYRACALKWHPDRHhtSTKNEAEEKFKLCTVAYQSLCEK 250
Cdd:PRK14288  16 NQETIKKSYRKLALKYHPDRN--AGDKEAEEKFKLINEAYGVLSDE 59
PRK14276 PRK14276
chaperone protein DnaJ; Provisional
 188-250 4.44e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 237653 [Multi-domain]  Cd Length: 380  Bit Score: 40.84  E-value: 4.44e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 186511163 188 NQESHRQTLGLSSSGplNLEDVKIAYRACALKWHPDRHHTStknEAEEKFKLCTVAYQSLCEK 250
Cdd:PRK14276   2 NNTEYYDRLGVSKDA--SQDEIKKAYRKLSKKYHPDINKEP---GAEEKYKEVQEAYETLSDP 59
PRK14285 PRK14285
chaperone protein DnaJ; Provisional
 189-247 4.93e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 172773 [Multi-domain]  Cd Length: 365  Bit Score: 40.75  E-value: 4.93e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 186511163 189 QESHRQTLGLSSSGplNLEDVKIAYRACALKWHPDRHHTStkNEAEEKFKLCTVAYQSL 247
Cdd:PRK14285   2 KRDYYEILGLSKGA--SKDEIKKAYRKIAIKYHPDKNKGN--KEAESIFKEATEAYEVL 56
PRK14277 PRK14277
chaperone protein DnaJ; Provisional
 207-247 5.68e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 184599 [Multi-domain]  Cd Length: 386  Bit Score: 40.55  E-value: 5.68e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 186511163 207 EDVKIAYRACALKWHPDRHHTSTknEAEEKFKLCTVAYQSL 247
Cdd:PRK14277  20 EEIKKAYRRLAKKYHPDLNPGDK--EAEQKFKEINEAYEIL 58
PRK14279 PRK14279
molecular chaperone DnaJ;
196-247 8.16e-04

molecular chaperone DnaJ;


Pssm-ID: 237655 [Multi-domain]  Cd Length: 392  Bit Score: 40.10  E-value: 8.16e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 186511163 196 LGLSSSGplNLEDVKIAYRACALKWHPDRHHTSTKneAEEKFKLCTVAYQSL 247
Cdd:PRK14279  15 LGVSSDA--SAEEIKKAYRKLARELHPDANPGDPA--AEERFKAVSEAHDVL 62
PRK14284 PRK14284
chaperone protein DnaJ; Provisional
 207-247 8.64e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 237658 [Multi-domain]  Cd Length: 391  Bit Score: 40.21  E-value: 8.64e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 186511163 207 EDVKIAYRACALKWHPDRHhtSTKNEAEEKFKLCTVAYQSL 247
Cdd:PRK14284  16 EEIKKAYRKLAVKYHPDKN--PGDAEAEKRFKEVSEAYEVL 54
PRK14289 PRK14289
molecular chaperone DnaJ;
194-247 8.82e-04

molecular chaperone DnaJ;


Pssm-ID: 237660 [Multi-domain]  Cd Length: 386  Bit Score: 40.20  E-value: 8.82e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 186511163 194 QTLGLSSSGplNLEDVKIAYRACALKWHPDRHHTStkNEAEEKFKLCTVAYQSL 247
Cdd:PRK14289   9 EVLGVSKTA--TVDEIKKAYRKKAIQYHPDKNPGD--KEAEEKFKEAAEAYDVL 58
PRK14293 PRK14293
molecular chaperone DnaJ;
194-249 1.96e-03

molecular chaperone DnaJ;


Pssm-ID: 237663 [Multi-domain]  Cd Length: 374  Bit Score: 38.82  E-value: 1.96e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 186511163 194 QTLGLSSSGplNLEDVKIAYRACALKWHPDrhhTSTKNEAEEKFKLCTVAYQSLCE 249
Cdd:PRK14293   7 EILGVSRDA--DKDELKRAYRRLARKYHPD---VNKEPGAEDRFKEINRAYEVLSD 57
PRK14280 PRK14280
molecular chaperone DnaJ;
196-247 4.27e-03

molecular chaperone DnaJ;


Pssm-ID: 237656 [Multi-domain]  Cd Length: 376  Bit Score: 37.78  E-value: 4.27e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 186511163 196 LGLSSSGplNLEDVKIAYRACALKWHPDrhhTSTKNEAEEKFKLCTVAYQSL 247
Cdd:PRK14280  10 LGVSKSA--SKDEIKKAYRKLSKKYHPD---INKEEGADEKFKEISEAYEVL 56
 
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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