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Conserved domains on  [gi|334186708|ref|NP_193693|]
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DNAJ heat shock N-terminal domain-containing protein [Arabidopsis thaliana]

Protein Classification

J domain-containing protein( domain architecture ID 10446266)

J domain-containing protein containing a similar domain as 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 pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 66-119 3.26e-16

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: 71.74  E-value: 3.26e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 334186708   66 DWYGILGIDPLADEEAVKKQYKKLALLLHPDKNRFN-GAEGAFKLVRHARDLLSD 119
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNPGDpEAEEKFKEINEAYEVLSD 55
 
Name Accession Description Interval E-value
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 66-119 3.26e-16

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: 71.74  E-value: 3.26e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 334186708   66 DWYGILGIDPLADEEAVKKQYKKLALLLHPDKNRFN-GAEGAFKLVRHARDLLSD 119
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNPGDpEAEEKFKEINEAYEVLSD 55
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 66-119 9.11e-15

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: 67.57  E-value: 9.11e-15
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 334186708  66 DWYGILGIDPLADEEAVKKQYKKLALLLHPDKNRFN-GAEGAFKLVRHARDLLSD 119
Cdd:cd06257    1 DYYDILGVPPDASDEEIKKAYRKLALKYHPDKNPDDpEAEEKFKEINEAYEVLSD 55
DnaJ smart00271
DnaJ molecular chaperone homology domain;
66-120 6.17e-13

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 62.64  E-value: 6.17e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 334186708    66 DWYGILGIDPLADEEAVKKQYKKLALLLHPDKNRFN--GAEGAFKLVRHARDLLSDQ 120
Cdd:smart00271   2 DYYEILGVPRDASLDEIKKAYRKLALKYHPDKNPGDkeEAEEKFKEINEAYEVLSDP 58
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 66-119 1.73e-12

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: 63.95  E-value: 1.73e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 334186708  66 DWYGILGIDPLADEEAVKKQYKKLALLLHPDKNRFN-GAEGAFKLVRHARDLLSD 119
Cdd:COG0484    1 DYYEILGVSRDASAEEIKKAYRKLAKKYHPDRNPGDpEAEEKFKEINEAYEVLSD 55
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 66-119 1.96e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 60.93  E-value: 1.96e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 334186708  66 DWYGILGIDPLADEEAVKKQYKKLALLLHPDKNRFN-GAEGAFKLVRHARDLLSD 119
Cdd:PRK10767   5 DYYEVLGVSRNASEDEIKKAYRKLAMKYHPDRNPGDkEAEEKFKEIKEAYEVLSD 59
 
Name Accession Description Interval E-value
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 66-119 3.26e-16

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: 71.74  E-value: 3.26e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 334186708   66 DWYGILGIDPLADEEAVKKQYKKLALLLHPDKNRFN-GAEGAFKLVRHARDLLSD 119
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNPGDpEAEEKFKEINEAYEVLSD 55
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 66-119 9.11e-15

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: 67.57  E-value: 9.11e-15
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 334186708  66 DWYGILGIDPLADEEAVKKQYKKLALLLHPDKNRFN-GAEGAFKLVRHARDLLSD 119
Cdd:cd06257    1 DYYDILGVPPDASDEEIKKAYRKLALKYHPDKNPDDpEAEEKFKEINEAYEVLSD 55
DnaJ smart00271
DnaJ molecular chaperone homology domain;
66-120 6.17e-13

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 62.64  E-value: 6.17e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 334186708    66 DWYGILGIDPLADEEAVKKQYKKLALLLHPDKNRFN--GAEGAFKLVRHARDLLSDQ 120
Cdd:smart00271   2 DYYEILGVPRDASLDEIKKAYRKLALKYHPDKNPGDkeEAEEKFKEINEAYEVLSDP 58
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 66-119 1.73e-12

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: 63.95  E-value: 1.73e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 334186708  66 DWYGILGIDPLADEEAVKKQYKKLALLLHPDKNRFN-GAEGAFKLVRHARDLLSD 119
Cdd:COG0484    1 DYYEILGVSRDASAEEIKKAYRKLAKKYHPDRNPGDpEAEEKFKEINEAYEVLSD 55
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 66-119 1.96e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 60.93  E-value: 1.96e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 334186708  66 DWYGILGIDPLADEEAVKKQYKKLALLLHPDKNRFN-GAEGAFKLVRHARDLLSD 119
Cdd:PRK10767   5 DYYEVLGVSRNASEDEIKKAYRKLAMKYHPDRNPGDkEAEEKFKEIKEAYEVLSD 59
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
 66-119 3.52e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 60.25  E-value: 3.52e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 334186708  66 DWYGILGIDPLADEEAVKKQYKKLALLLHPDKNRFNGAEGAFKLVRHARDLLSD 119
Cdd:PRK14298   6 DYYEILGLSKDASVEDIKKAYRKLAMKYHPDKNKEPDAEEKFKEISEAYAVLSD 59
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
64-119 5.45e-10

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


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 55.49  E-value: 5.45e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 334186708  64 EADWYGILGIDPLADEEAVKKQYKKLALLLHPDKNRFNG--AEGAFKLVRHARDLLSD 119
Cdd:COG2214    4 LKDHYAVLGVPPDASLEEIRQAYRRLAKLLHPDRGGELKalAEELFQRLNEAYEVLSD 61
PRK14283 PRK14283
chaperone protein DnaJ; Provisional
 66-119 3.20e-09

chaperone protein DnaJ; Provisional


Pssm-ID: 184604 [Multi-domain]  Cd Length: 378  Bit Score: 57.53  E-value: 3.20e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 334186708  66 DWYGILGIDPLADEEAVKKQYKKLALLLHPDKNRFNGAEGAFKLVRHARDLLSD 119
Cdd:PRK14283   6 DYYEVLGVDRNADKKEIKKAYRKLARKYHPDVSEEEGAEEKFKEISEAYAVLSD 59
PRK14279 PRK14279
molecular chaperone DnaJ;
64-119 4.23e-09

molecular chaperone DnaJ;


Pssm-ID: 237655 [Multi-domain]  Cd Length: 392  Bit Score: 57.05  E-value: 4.23e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 334186708  64 EADWYGILGIDPLADEEAVKKQYKKLALLLHPDKNRFN-GAEGAFKLVRHARDLLSD 119
Cdd:PRK14279   8 EKDFYKELGVSSDASAEEIKKAYRKLARELHPDANPGDpAAEERFKAVSEAHDVLSD 64
PRK14299 PRK14299
chaperone protein DnaJ; Provisional
 66-119 7.18e-09

chaperone protein DnaJ; Provisional


Pssm-ID: 237667 [Multi-domain]  Cd Length: 291  Bit Score: 55.72  E-value: 7.18e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 334186708  66 DWYGILGIDPLADEEAVKKQYKKLALLLHPDKNRFNGAEGAFKLVRHARDLLSD 119
Cdd:PRK14299   5 DYYAILGVPKNASQDEIKKAFKKLARKYHPDVNKSPGAEEKFKEINEAYTVLSD 58
PRK14295 PRK14295
molecular chaperone DnaJ;
64-120 9.87e-09

molecular chaperone DnaJ;


Pssm-ID: 237665 [Multi-domain]  Cd Length: 389  Bit Score: 56.01  E-value: 9.87e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 334186708  64 EADWYGILGIDPLADEEAVKKQYKKLALLLHPDKNRFN-GAEGAFKLVRHARDLLSDQ 120
Cdd:PRK14295   8 EKDYYKVLGVPKDATEAEIKKAYRKLAREYHPDANKGDaKAEERFKEISEAYDVLSDE 65
PRK14293 PRK14293
molecular chaperone DnaJ;
65-119 1.59e-08

molecular chaperone DnaJ;


Pssm-ID: 237663 [Multi-domain]  Cd Length: 374  Bit Score: 55.38  E-value: 1.59e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 334186708  65 ADWYGILGIDPLADEEAVKKQYKKLALLLHPDKNRFNGAEGAFKLVRHARDLLSD 119
Cdd:PRK14293   3 ADYYEILGVSRDADKDELKRAYRRLARKYHPDVNKEPGAEDRFKEINRAYEVLSD 57
PRK14292 PRK14292
chaperone protein DnaJ; Provisional
 65-119 1.93e-08

chaperone protein DnaJ; Provisional


Pssm-ID: 237662 [Multi-domain]  Cd Length: 371  Bit Score: 54.90  E-value: 1.93e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 334186708  65 ADWYGILGIDPLADEEAVKKQYKKLALLLHPDKNRFNGAEGAFKLVRHARDLLSD 119
Cdd:PRK14292   2 MDYYELLGVSRTASADEIKSAYRKLALKYHPDRNKEKGAAEKFAQINEAYAVLSD 56
PRK14287 PRK14287
chaperone protein DnaJ; Provisional
 66-119 2.34e-08

chaperone protein DnaJ; Provisional


Pssm-ID: 237659 [Multi-domain]  Cd Length: 371  Bit Score: 54.63  E-value: 2.34e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 334186708  66 DWYGILGIDPLADEEAVKKQYKKLALLLHPDKNRFNGAEGAFKLVRHARDLLSD 119
Cdd:PRK14287   5 DYYEVLGVDRNASVDEVKKAYRKLARKYHPDVNKAPDAEDKFKEVKEAYDTLSD 58
PRK14297 PRK14297
molecular chaperone DnaJ;
66-119 2.39e-08

molecular chaperone DnaJ;


Pssm-ID: 184611 [Multi-domain]  Cd Length: 380  Bit Score: 54.79  E-value: 2.39e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 334186708  66 DWYGILGIDPLADEEAVKKQYKKLALLLHPDKNRFNG-AEGAFKLVRHARDLLSD 119
Cdd:PRK14297   5 DYYEVLGLEKGASDDEIKKAFRKLAIKYHPDKNKGNKeAEEKFKEINEAYQVLSD 59
PRK14276 PRK14276
chaperone protein DnaJ; Provisional
 64-119 2.62e-08

chaperone protein DnaJ; Provisional


Pssm-ID: 237653 [Multi-domain]  Cd Length: 380  Bit Score: 54.71  E-value: 2.62e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 334186708  64 EADWYGILGIDPLADEEAVKKQYKKLALLLHPDKNRFNGAEGAFKLVRHARDLLSD 119
Cdd:PRK14276   3 NTEYYDRLGVSKDASQDEIKKAYRKLSKKYHPDINKEPGAEEKYKEVQEAYETLSD 58
PRK14281 PRK14281
chaperone protein DnaJ; Provisional
 66-119 5.97e-08

chaperone protein DnaJ; Provisional


Pssm-ID: 237657 [Multi-domain]  Cd Length: 397  Bit Score: 53.66  E-value: 5.97e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 334186708  66 DWYGILGIDPLADEEAVKKQYKKLALLLHPDKNRFNG-AEGAFKLVRHARDLLSD 119
Cdd:PRK14281   4 DYYEVLGVSRSADKDEIKKAYRKLALKYHPDKNPDNKeAEEHFKEVNEAYEVLSN 58
PRK14278 PRK14278
chaperone protein DnaJ; Provisional
 66-119 5.99e-08

chaperone protein DnaJ; Provisional


Pssm-ID: 237654 [Multi-domain]  Cd Length: 378  Bit Score: 53.52  E-value: 5.99e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 334186708  66 DWYGILGIDPLADEEAVKKQYKKLALLLHPDKNRFNGAEGAFKLVRHARDLLSD 119
Cdd:PRK14278   4 DYYGLLGVSRNASDAEIKRAYRKLARELHPDVNPDEEAQEKFKEISVAYEVLSD 57
PRK14284 PRK14284
chaperone protein DnaJ; Provisional
 65-119 1.22e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 237658 [Multi-domain]  Cd Length: 391  Bit Score: 52.54  E-value: 1.22e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 334186708  65 ADWYGILGIDPLADEEAVKKQYKKLALLLHPDKNRFNG-AEGAFKLVRHARDLLSD 119
Cdd:PRK14284   1 MDYYTILGVSKTASPEEIKKAYRKLAVKYHPDKNPGDAeAEKRFKEVSEAYEVLSD 56
PRK14277 PRK14277
chaperone protein DnaJ; Provisional
 66-119 1.22e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 184599 [Multi-domain]  Cd Length: 386  Bit Score: 52.50  E-value: 1.22e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 334186708  66 DWYGILGIDPLADEEAVKKQYKKLALLLHPDKNRFN-GAEGAFKLVRHARDLLSD 119
Cdd:PRK14277   6 DYYEILGVDRNATEEEIKKAYRRLAKKYHPDLNPGDkEAEQKFKEINEAYEILSD 60
PRK14294 PRK14294
chaperone protein DnaJ; Provisional
 63-119 1.24e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 237664 [Multi-domain]  Cd Length: 366  Bit Score: 52.46  E-value: 1.24e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 334186708  63 GEADWYGILGIDPLADEEAVKKQYKKLALLLHPDKNRFNG-AEGAFKLVRHARDLLSD 119
Cdd:PRK14294   2 VKRDYYEILGVTRDASEEEIKKSYRKLAMKYHPDRNPGDKeAEELFKEAAEAYEVLSD 59
PRK14280 PRK14280
molecular chaperone DnaJ;
66-119 1.51e-07

molecular chaperone DnaJ;


Pssm-ID: 237656 [Multi-domain]  Cd Length: 376  Bit Score: 52.03  E-value: 1.51e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 334186708  66 DWYGILGIDPLADEEAVKKQYKKLALLLHPDKNRFNGAEGAFKLVRHARDLLSD 119
Cdd:PRK14280   5 DYYEVLGVSKSASKDEIKKAYRKLSKKYHPDINKEEGADEKFKEISEAYEVLSD 58
PRK10266 PRK10266
curved DNA-binding protein;
66-120 2.31e-07

curved DNA-binding protein;


Pssm-ID: 182347 [Multi-domain]  Cd Length: 306  Bit Score: 51.36  E-value: 2.31e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 334186708  66 DWYGILGIDPLADEEAVKKQYKKLALLLHPDKNRFNGAEGAFKLVRHARDLLSDQ 120
Cdd:PRK10266   5 DYYAIMGVKPTDDLKTIKTAYRRLARKYHPDVSKEPDAEARFKEVAEAWEVLSDE 59
PRK14301 PRK14301
chaperone protein DnaJ; Provisional
 66-119 3.78e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 237668 [Multi-domain]  Cd Length: 373  Bit Score: 50.90  E-value: 3.78e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 334186708  66 DWYGILGIDPLADEEAVKKQYKKLALLLHPDKNRFNG-AEGAFKLVRHARDLLSD 119
Cdd:PRK14301   5 DYYEVLGVSRDASEDEIKKAYRKLALQYHPDRNPDNPeAEQKFKEAAEAYEVLRD 59
PRK14289 PRK14289
molecular chaperone DnaJ;
66-119 6.50e-07

molecular chaperone DnaJ;


Pssm-ID: 237660 [Multi-domain]  Cd Length: 386  Bit Score: 50.21  E-value: 6.50e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 334186708  66 DWYGILGIDPLADEEAVKKQYKKLALLLHPDKNRFNG-AEGAFKLVRHARDLLSD 119
Cdd:PRK14289   6 DYYEVLGVSKTATVDEIKKAYRKKAIQYHPDKNPGDKeAEEKFKEAAEAYDVLSD 60
PRK14291 PRK14291
chaperone protein DnaJ; Provisional
 66-119 8.50e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 237661 [Multi-domain]  Cd Length: 382  Bit Score: 49.77  E-value: 8.50e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 334186708  66 DWYGILGIDPLADEEAVKKQYKKLALLLHPDKNRFNGAEGAFKLVRHARDLLSD 119
Cdd:PRK14291   4 DYYEILGVSRNATQEEIKKAYRRLARKYHPDFNKNPEAEEKFKEINEAYQVLSD 57
PRK14286 PRK14286
chaperone protein DnaJ; Provisional
 64-119 1.52e-06

chaperone protein DnaJ; Provisional


Pssm-ID: 172774 [Multi-domain]  Cd Length: 372  Bit Score: 49.22  E-value: 1.52e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 334186708  64 EADWYGILGIDPLADEEAVKKQYKKLALLLHPDKNRFNG-AEGAFKLVRHARDLLSD 119
Cdd:PRK14286   3 ERSYYDILGVSKSANDEEIKSAYRKLAIKYHPDKNKGNKeSEEKFKEATEAYEILRD 59
PRK14296 PRK14296
chaperone protein DnaJ; Provisional
 66-120 2.62e-06

chaperone protein DnaJ; Provisional


Pssm-ID: 237666 [Multi-domain]  Cd Length: 372  Bit Score: 48.40  E-value: 2.62e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 334186708  66 DWYGILGIDPLADEEAVKKQYKKLALLLHPDKNRFNGAEGAFKLVRHARDLLSDQ 120
Cdd:PRK14296   5 DYYEVLGVSKTASEQEIRQAYRKLAKQYHPDLNKSPDAHDKMVEINEAADVLLDK 59
PRK14285 PRK14285
chaperone protein DnaJ; Provisional
 66-119 3.81e-06

chaperone protein DnaJ; Provisional


Pssm-ID: 172773 [Multi-domain]  Cd Length: 365  Bit Score: 48.06  E-value: 3.81e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 334186708  66 DWYGILGIDPLADEEAVKKQYKKLALLLHPDKNRFNG-AEGAFKLVRHARDLLSD 119
Cdd:PRK14285   4 DYYEILGLSKGASKDEIKKAYRKIAIKYHPDKNKGNKeAESIFKEATEAYEVLID 58
PRK14290 PRK14290
chaperone protein DnaJ; Provisional
 66-131 6.70e-06

chaperone protein DnaJ; Provisional


Pssm-ID: 172778 [Multi-domain]  Cd Length: 365  Bit Score: 47.23  E-value: 6.70e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334186708  66 DWYGILGIDPLADEEAVKKQYKKLALLLHPDKNRFNG--AEGAFKLVRHARDLLSD-QPCLIYNVQGQT 131
Cdd:PRK14290   4 DYYKILGVDRNASQEDIKKAFRELAKKWHPDLHPGNKaeAEEKFKEISEAYEVLSDpQKRRQYDQTGTV 72
PRK14282 PRK14282
chaperone protein DnaJ; Provisional
 66-119 1.05e-05

chaperone protein DnaJ; Provisional


Pssm-ID: 184603 [Multi-domain]  Cd Length: 369  Bit Score: 46.71  E-value: 1.05e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 334186708  66 DWYGILGIDPLADEEAVKKQYKKLALLLHPDKNRFNG--AEGAFKLVRHARDLLSD 119
Cdd:PRK14282   5 DYYEILGVSRNATQEEIKRAYKRLVKEWHPDRHPENRkeAEQKFKEIQEAYEVLSD 60
PRK14300 PRK14300
chaperone protein DnaJ; Provisional
 66-120 1.64e-05

chaperone protein DnaJ; Provisional


Pssm-ID: 172788 [Multi-domain]  Cd Length: 372  Bit Score: 45.78  E-value: 1.64e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 334186708  66 DWYGILGIDPLADEEAVKKQYKKLALLLHPDKNRFNGAEGAFKLVRHARDLLSDQ 120
Cdd:PRK14300   4 DYYQILGVSKTASQADLKKAYLKLAKQYHPDTTDAKDAEKKFKEINAAYDVLKDE 58
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
63-97 2.76e-05

DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 41.71  E-value: 2.76e-05
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 334186708  63 GEADWYGILGIDPLADEEAVKKQYKKLALLLHPDK 97
Cdd:COG1076    2 QLDDAFELLGLPPDADDAELKRAYRKLQREHHPDR 36
PRK14288 PRK14288
molecular chaperone DnaJ;
64-138 5.58e-05

molecular chaperone DnaJ;


Pssm-ID: 172776 [Multi-domain]  Cd Length: 369  Bit Score: 44.29  E-value: 5.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186708  64 EADWYGILGIDPLADEEAVKKQYKKLALLLHPDKNRFNG-AEGAFKLVRHARDLLSDQPCLI----YNVQGQTQTQKSQN 138
Cdd:PRK14288   2 ELSYYEILEVEKHSNQETIKKSYRKLALKYHPDRNAGDKeAEEKFKLINEAYGVLSDEKKRAlydrYGKKGLNQAGASQS 81
ZUO1 COG5269
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ...
 63-119 6.26e-04

Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227594 [Multi-domain]  Cd Length: 379  Bit Score: 41.17  E-value: 6.26e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334186708  63 GEADWYGILGIDPL---ADEEAVKKQYKKLALLLHPDKNRFNGA---EGAFKLVRHARDLLSD 119
Cdd:COG5269   41 KKVDLYALLGLSKYrtkAIPPQILKAHKKKVYKYHPDKTAAGGNkgcDEFFKLIQKAREVLGD 103
PTZ00037 PTZ00037
DnaJ_C chaperone protein; Provisional
 68-119 2.26e-03

DnaJ_C chaperone protein; Provisional


Pssm-ID: 240236 [Multi-domain]  Cd Length: 421  Bit Score: 39.42  E-value: 2.26e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 334186708  68 YGILGIDPLADEEAVKKQYKKLALLLHPDKnrfNGAEGAFKLVRHARDLLSD 119
Cdd:PTZ00037  31 YEVLNLSKDCTTSEIKKAYRKLAIKHHPDK---GGDPEKFKEISRAYEVLSD 79
 
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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