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Conserved domains on  [gi|15240208|ref|NP_198554|]
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Chaperone DnaJ-domain superfamily 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
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 ...
66-127 1.46e-21

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: 87.53  E-value: 1.46e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15240208    66 DWYGILNASPRDDDETLKRKYRKLALMLHPDKN-KSIGAEGAFKHVSEAWKFLSDKEKRAAYD 127
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNpGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
 
Name Accession Description Interval E-value
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
66-127 1.46e-21

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: 87.53  E-value: 1.46e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15240208    66 DWYGILNASPRDDDETLKRKYRKLALMLHPDKN-KSIGAEGAFKHVSEAWKFLSDKEKRAAYD 127
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNpGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
66-128 2.79e-18

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 86.06  E-value: 2.79e-18
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15240208   66 DWYGILNASPRDDDETLKRKYRKLALMLHPDKNKSIGAEGAFKHVSEAWKFLSDKEKRAAYDR 128
Cdd:PRK14298   6 DYYEILGLSKDASVEDIKKAYRKLAMKYHPDKNKEPDAEEKFKEISEAYAVLSDAEKRAQYDR 68
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
66-128 1.01e-17

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: 79.36  E-value: 1.01e-17
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15240208  66 DWYGILNASPRDDDETLKRKYRKLALMLHPDKNKS-IGAEGAFKHVSEAWKFLSDKEKRAAYDR 128
Cdd:COG0484   1 DYYEILGVSRDASAEEIKKAYRKLAKKYHPDRNPGdPEAEEKFKEINEAYEVLSDPEKRAAYDR 64
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
66-128 1.47e-17

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: 83.42  E-value: 1.47e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15240208    66 DWYGILNASPRDDDETLKRKYRKLALMLHPDKNKSIGAEGAFKHVSEAWKFLSDKEKRAAYDR 128
Cdd:TIGR02349   1 DYYEILGVSKDASEEEIKKAYRKLAKKYHPDRNKDKEAEEKFKEINEAYEVLSDPEKRAQYDQ 63
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
66-119 1.18e-16

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: 73.73  E-value: 1.18e-16
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15240208  66 DWYGILNASPRDDDETLKRKYRKLALMLHPDKNKSI-GAEGAFKHVSEAWKFLSD 119
Cdd:cd06257   1 DYYDILGVPPDASDEEIKKAYRKLALKYHPDKNPDDpEAEEKFKEINEAYEVLSD 55
DnaJ smart00271
DnaJ molecular chaperone homology domain;
65-122 6.61e-16

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 71.50  E-value: 6.61e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240208     65 VDWYGILNASPRDDDETLKRKYRKLALMLHPDKNKS--IGAEGAFKHVSEAWKFLSDKEK 122
Cdd:smart00271   1 TDYYEILGVPRDASLDEIKKAYRKLALKYHPDKNPGdkEEAEEKFKEINEAYEVLSDPEK 60
terminal_TopJ NF037946
terminal organelle assembly protein TopJ;
66-128 7.69e-15

terminal organelle assembly protein TopJ;


Pssm-ID: 468284 [Multi-domain]  Cd Length: 440  Bit Score: 76.01  E-value: 7.69e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15240208   66 DWYGILNASPRDDDETLKRKYRKLALMLHPDKNKSIGAEGAFKHVSEAWKFLSDKEKRAAYDR 128
Cdd:NF037946   6 DYYEVLGVDRDADDQEIKKAFRKLAKKYHPDRNKAPDAAEIFAEINEAYEVLSNPEKRANYDK 68
 
Name Accession Description Interval E-value
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
66-127 1.46e-21

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: 87.53  E-value: 1.46e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15240208    66 DWYGILNASPRDDDETLKRKYRKLALMLHPDKN-KSIGAEGAFKHVSEAWKFLSDKEKRAAYD 127
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNpGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
66-128 2.79e-18

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 86.06  E-value: 2.79e-18
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15240208   66 DWYGILNASPRDDDETLKRKYRKLALMLHPDKNKSIGAEGAFKHVSEAWKFLSDKEKRAAYDR 128
Cdd:PRK14298   6 DYYEILGLSKDASVEDIKKAYRKLAMKYHPDKNKEPDAEEKFKEISEAYAVLSDAEKRAQYDR 68
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
66-128 1.01e-17

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: 79.36  E-value: 1.01e-17
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15240208  66 DWYGILNASPRDDDETLKRKYRKLALMLHPDKNKS-IGAEGAFKHVSEAWKFLSDKEKRAAYDR 128
Cdd:COG0484   1 DYYEILGVSRDASAEEIKKAYRKLAKKYHPDRNPGdPEAEEKFKEINEAYEVLSDPEKRAAYDR 64
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
66-128 1.47e-17

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: 83.42  E-value: 1.47e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15240208    66 DWYGILNASPRDDDETLKRKYRKLALMLHPDKNKSIGAEGAFKHVSEAWKFLSDKEKRAAYDR 128
Cdd:TIGR02349   1 DYYEILGVSKDASEEEIKKAYRKLAKKYHPDRNKDKEAEEKFKEINEAYEVLSDPEKRAQYDQ 63
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
66-128 9.45e-17

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 81.34  E-value: 9.45e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15240208   66 DWYGILNASPRDDDETLKRKYRKLALMLHPDKNK-SIGAEGAFKHVSEAWKFLSDKEKRAAYDR 128
Cdd:PRK10767   5 DYYEVLGVSRNASEDEIKKAYRKLAMKYHPDRNPgDKEAEEKFKEIKEAYEVLSDPQKRAAYDQ 68
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
66-119 1.18e-16

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: 73.73  E-value: 1.18e-16
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15240208  66 DWYGILNASPRDDDETLKRKYRKLALMLHPDKNKSI-GAEGAFKHVSEAWKFLSD 119
Cdd:cd06257   1 DYYDILGVPPDASDEEIKKAYRKLALKYHPDKNPDDpEAEEKFKEINEAYEVLSD 55
DnaJ smart00271
DnaJ molecular chaperone homology domain;
65-122 6.61e-16

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 71.50  E-value: 6.61e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240208     65 VDWYGILNASPRDDDETLKRKYRKLALMLHPDKNKS--IGAEGAFKHVSEAWKFLSDKEK 122
Cdd:smart00271   1 TDYYEILGVPRDASLDEIKKAYRKLALKYHPDKNPGdkEEAEEKFKEINEAYEVLSDPEK 60
PRK14293 PRK14293
molecular chaperone DnaJ;
66-128 6.88e-16

molecular chaperone DnaJ;


Pssm-ID: 237663 [Multi-domain]  Cd Length: 374  Bit Score: 78.88  E-value: 6.88e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15240208   66 DWYGILNASPRDDDETLKRKYRKLALMLHPDKNKSIGAEGAFKHVSEAWKFLSDKEKRAAYDR 128
Cdd:PRK14293   4 DYYEILGVSRDADKDELKRAYRRLARKYHPDVNKEPGAEDRFKEINRAYEVLSDPETRARYDQ 66
PRK14292 PRK14292
chaperone protein DnaJ; Provisional
65-128 6.42e-15

chaperone protein DnaJ; Provisional


Pssm-ID: 237662 [Multi-domain]  Cd Length: 371  Bit Score: 75.70  E-value: 6.42e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15240208   65 VDWYGILNASPRDDDETLKRKYRKLALMLHPDKNKSIGAEGAFKHVSEAWKFLSDKEKRAAYDR 128
Cdd:PRK14292   2 MDYYELLGVSRTASADEIKSAYRKLALKYHPDRNKEKGAAEKFAQINEAYAVLSDAEKRAHYDR 65
PRK14276 PRK14276
chaperone protein DnaJ; Provisional
66-127 6.62e-15

chaperone protein DnaJ; Provisional


Pssm-ID: 237653 [Multi-domain]  Cd Length: 380  Bit Score: 75.89  E-value: 6.62e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15240208   66 DWYGILNASPRDDDETLKRKYRKLALMLHPDKNKSIGAEGAFKHVSEAWKFLSDKEKRAAYD 127
Cdd:PRK14276   5 EYYDRLGVSKDASQDEIKKAYRKLSKKYHPDINKEPGAEEKYKEVQEAYETLSDPQKRAAYD 66
PRK10266 PRK10266
curved DNA-binding protein;
66-128 7.65e-15

curved DNA-binding protein;


Pssm-ID: 182347 [Multi-domain]  Cd Length: 306  Bit Score: 74.86  E-value: 7.65e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15240208   66 DWYGILNASPRDDDETLKRKYRKLALMLHPDKNKSIGAEGAFKHVSEAWKFLSDKEKRAAYDR 128
Cdd:PRK10266   5 DYYAIMGVKPTDDLKTIKTAYRRLARKYHPDVSKEPDAEARFKEVAEAWEVLSDEQRRAEYDQ 67
terminal_TopJ NF037946
terminal organelle assembly protein TopJ;
66-128 7.69e-15

terminal organelle assembly protein TopJ;


Pssm-ID: 468284 [Multi-domain]  Cd Length: 440  Bit Score: 76.01  E-value: 7.69e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15240208   66 DWYGILNASPRDDDETLKRKYRKLALMLHPDKNKSIGAEGAFKHVSEAWKFLSDKEKRAAYDR 128
Cdd:NF037946   6 DYYEVLGVDRDADDQEIKKAFRKLAKKYHPDRNKAPDAAEIFAEINEAYEVLSNPEKRANYDK 68
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
66-129 5.55e-14

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


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 67.05  E-value: 5.55e-14
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15240208  66 DWYGILNASPRDDDETLKRKYRKLALMLHPDKNKSIG--AEGAFKHVSEAWKFLSDKEKRAAYDRR 129
Cdd:COG2214   6 DHYAVLGVPPDASLEEIRQAYRRLAKLLHPDRGGELKalAEELFQRLNEAYEVLSDPERRAEYDRE 71
PRK14299 PRK14299
chaperone protein DnaJ; Provisional
66-128 1.40e-13

chaperone protein DnaJ; Provisional


Pssm-ID: 237667 [Multi-domain]  Cd Length: 291  Bit Score: 70.74  E-value: 1.40e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15240208   66 DWYGILNASPRDDDETLKRKYRKLALMLHPDKNKSIGAEGAFKHVSEAWKFLSDKEKRAAYDR 128
Cdd:PRK14299   5 DYYAILGVPKNASQDEIKKAFKKLARKYHPDVNKSPGAEEKFKEINEAYTVLSDPEKRRIYDT 67
PRK14283 PRK14283
chaperone protein DnaJ; Provisional
66-128 1.67e-13

chaperone protein DnaJ; Provisional


Pssm-ID: 184604 [Multi-domain]  Cd Length: 378  Bit Score: 71.39  E-value: 1.67e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15240208   66 DWYGILNASPRDDDETLKRKYRKLALMLHPDKNKSIGAEGAFKHVSEAWKFLSDKEKRAAYDR 128
Cdd:PRK14283   6 DYYEVLGVDRNADKKEIKKAYRKLARKYHPDVSEEEGAEEKFKEISEAYAVLSDDEKRQRYDQ 68
PRK14280 PRK14280
molecular chaperone DnaJ;
66-128 2.48e-13

molecular chaperone DnaJ;


Pssm-ID: 237656 [Multi-domain]  Cd Length: 376  Bit Score: 70.91  E-value: 2.48e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15240208   66 DWYGILNASPRDDDETLKRKYRKLALMLHPDKNKSIGAEGAFKHVSEAWKFLSDKEKRAAYDR 128
Cdd:PRK14280   5 DYYEVLGVSKSASKDEIKKAYRKLSKKYHPDINKEEGADEKFKEISEAYEVLSDDQKRAQYDQ 67
PRK14301 PRK14301
chaperone protein DnaJ; Provisional
66-128 1.46e-12

chaperone protein DnaJ; Provisional


Pssm-ID: 237668 [Multi-domain]  Cd Length: 373  Bit Score: 68.62  E-value: 1.46e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15240208   66 DWYGILNASPRDDDETLKRKYRKLALMLHPDKN-KSIGAEGAFKHVSEAWKFLSDKEKRAAYDR 128
Cdd:PRK14301   5 DYYEVLGVSRDASEDEIKKAYRKLALQYHPDRNpDNPEAEQKFKEAAEAYEVLRDAEKRARYDR 68
SEC63 COG5407
Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular ...
66-125 2.36e-12

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


Pssm-ID: 444165 [Multi-domain]  Cd Length: 61  Bit Score: 61.55  E-value: 2.36e-12
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15240208  66 DWYGILNASPRDDDETLKRKYRKLALMLHPDKNK-SIGAEGAFKHVSEAWKFLSDKEKRAA 125
Cdd:COG5407   1 DPYEVLGVAKTASADEIKKAYRKLAKKYHPDRNKgDPKAEERFKEINEAYELLSDAEKRAR 61
PRK14286 PRK14286
chaperone protein DnaJ; Provisional
64-148 4.07e-12

chaperone protein DnaJ; Provisional


Pssm-ID: 172774 [Multi-domain]  Cd Length: 372  Bit Score: 67.32  E-value: 4.07e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240208   64 DVDWYGILNASPRDDDETLKRKYRKLALMLHPDKNK-SIGAEGAFKHVSEAWKFLSDKEKRAAYDRrkslhsvYQKVSVS 142
Cdd:PRK14286   3 ERSYYDILGVSKSANDEEIKSAYRKLAIKYHPDKNKgNKESEEKFKEATEAYEILRDPKKRQAYDQ-------FGKAGVN 75

                 ....*.
gi 15240208  143 SSNNGF 148
Cdd:PRK14286  76 AGAGGF 81
PRK14278 PRK14278
chaperone protein DnaJ; Provisional
66-127 4.26e-12

chaperone protein DnaJ; Provisional


Pssm-ID: 237654 [Multi-domain]  Cd Length: 378  Bit Score: 67.38  E-value: 4.26e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15240208   66 DWYGILNASPRDDDETLKRKYRKLALMLHPDKNKSIGAEGAFKHVSEAWKFLSDKEKRAAYD 127
Cdd:PRK14278   4 DYYGLLGVSRNASDAEIKRAYRKLARELHPDVNPDEEAQEKFKEISVAYEVLSDPEKRRIVD 65
PRK14291 PRK14291
chaperone protein DnaJ; Provisional
66-127 4.35e-12

chaperone protein DnaJ; Provisional


Pssm-ID: 237661 [Multi-domain]  Cd Length: 382  Bit Score: 67.10  E-value: 4.35e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15240208   66 DWYGILNASPRDDDETLKRKYRKLALMLHPDKNKSIGAEGAFKHVSEAWKFLSDKEKRAAYD 127
Cdd:PRK14291   4 DYYEILGVSRNATQEEIKKAYRRLARKYHPDFNKNPEAEEKFKEINEAYQVLSDPEKRKLYD 65
PRK14284 PRK14284
chaperone protein DnaJ; Provisional
66-128 5.63e-12

chaperone protein DnaJ; Provisional


Pssm-ID: 237658 [Multi-domain]  Cd Length: 391  Bit Score: 66.79  E-value: 5.63e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15240208   66 DWYGILNASPRDDDETLKRKYRKLALMLHPDKNK-SIGAEGAFKHVSEAWKFLSDKEKRAAYDR 128
Cdd:PRK14284   2 DYYTILGVSKTASPEEIKKAYRKLAVKYHPDKNPgDAEAEKRFKEVSEAYEVLSDAQKRESYDR 65
PRK14295 PRK14295
molecular chaperone DnaJ;
66-132 1.11e-11

molecular chaperone DnaJ;


Pssm-ID: 237665 [Multi-domain]  Cd Length: 389  Bit Score: 66.03  E-value: 1.11e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15240208   66 DWYGILNASPRDDDETLKRKYRKLALMLHPDKNK-SIGAEGAFKHVSEAWKFLSDKEKRAAYDRRKSL 132
Cdd:PRK14295  10 DYYKVLGVPKDATEAEIKKAYRKLAREYHPDANKgDAKAEERFKEISEAYDVLSDEKKRKEYDEARSL 77
PRK14297 PRK14297
molecular chaperone DnaJ;
66-128 1.41e-11

molecular chaperone DnaJ;


Pssm-ID: 184611 [Multi-domain]  Cd Length: 380  Bit Score: 65.57  E-value: 1.41e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15240208   66 DWYGILNASPRDDDETLKRKYRKLALMLHPDKNK-SIGAEGAFKHVSEAWKFLSDKEKRAAYDR 128
Cdd:PRK14297   5 DYYEVLGLEKGASDDEIKKAFRKLAIKYHPDKNKgNKEAEEKFKEINEAYQVLSDPQKKAQYDQ 68
PRK14294 PRK14294
chaperone protein DnaJ; Provisional
66-128 2.22e-11

chaperone protein DnaJ; Provisional


Pssm-ID: 237664 [Multi-domain]  Cd Length: 366  Bit Score: 64.79  E-value: 2.22e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15240208   66 DWYGILNASPRDDDETLKRKYRKLALMLHPDKNK-SIGAEGAFKHVSEAWKFLSDKEKRAAYDR 128
Cdd:PRK14294   5 DYYEILGVTRDASEEEIKKSYRKLAMKYHPDRNPgDKEAEELFKEAAEAYEVLSDPKKRGIYDQ 68
PRK14281 PRK14281
chaperone protein DnaJ; Provisional
66-128 2.84e-11

chaperone protein DnaJ; Provisional


Pssm-ID: 237657 [Multi-domain]  Cd Length: 397  Bit Score: 64.83  E-value: 2.84e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15240208   66 DWYGILNASPRDDDETLKRKYRKLALMLHPDKN-KSIGAEGAFKHVSEAWKFLSDKEKRAAYDR 128
Cdd:PRK14281   4 DYYEVLGVSRSADKDEIKKAYRKLALKYHPDKNpDNKEAEEHFKEVNEAYEVLSNDDKRRRYDQ 67
PRK14279 PRK14279
molecular chaperone DnaJ;
66-132 4.21e-11

molecular chaperone DnaJ;


Pssm-ID: 237655 [Multi-domain]  Cd Length: 392  Bit Score: 64.37  E-value: 4.21e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15240208   66 DWYGILNASPRDDDETLKRKYRKLALMLHPDKNK-SIGAEGAFKHVSEAWKFLSDKEKRAAYDRRKSL 132
Cdd:PRK14279  10 DFYKELGVSSDASAEEIKKAYRKLARELHPDANPgDPAAEERFKAVSEAHDVLSDPAKRKEYDETRRL 77
PRK14277 PRK14277
chaperone protein DnaJ; Provisional
66-128 4.29e-11

chaperone protein DnaJ; Provisional


Pssm-ID: 184599 [Multi-domain]  Cd Length: 386  Bit Score: 64.05  E-value: 4.29e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15240208   66 DWYGILNASPRDDDETLKRKYRKLALMLHPDKNK-SIGAEGAFKHVSEAWKFLSDKEKRAAYDR 128
Cdd:PRK14277   6 DYYEILGVDRNATEEEIKKAYRRLAKKYHPDLNPgDKEAEQKFKEINEAYEILSDPQKRAQYDQ 69
PRK14289 PRK14289
molecular chaperone DnaJ;
66-128 7.52e-11

molecular chaperone DnaJ;


Pssm-ID: 237660 [Multi-domain]  Cd Length: 386  Bit Score: 63.31  E-value: 7.52e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15240208   66 DWYGILNASPRDDDETLKRKYRKLALMLHPDKNK-SIGAEGAFKHVSEAWKFLSDKEKRAAYDR 128
Cdd:PRK14289   6 DYYEVLGVSKTATVDEIKKAYRKKAIQYHPDKNPgDKEAEEKFKEAAEAYDVLSDPDKRSRYDQ 69
PRK14296 PRK14296
chaperone protein DnaJ; Provisional
66-147 3.74e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 237666 [Multi-domain]  Cd Length: 372  Bit Score: 61.12  E-value: 3.74e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240208   66 DWYGILNASPRDDDETLKRKYRKLALMLHPDKNKSIGAEGAFKHVSEAWKFLSDKEKRAAYDRRKslHSVYQKVSVSSSN 145
Cdd:PRK14296   5 DYYEVLGVSKTASEQEIRQAYRKLAKQYHPDLNKSPDAHDKMVEINEAADVLLDKDKRKQYDQFG--HAAFDGSSGFSSN 82

                 ..
gi 15240208  146 NG 147
Cdd:PRK14296  83 FG 84
PRK14282 PRK14282
chaperone protein DnaJ; Provisional
66-128 7.35e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 184603 [Multi-domain]  Cd Length: 369  Bit Score: 60.19  E-value: 7.35e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15240208   66 DWYGILNASPRDDDETLKRKYRKLALMLHPDKN--KSIGAEGAFKHVSEAWKFLSDKEKRAAYDR 128
Cdd:PRK14282   5 DYYEILGVSRNATQEEIKRAYKRLVKEWHPDRHpeNRKEAEQKFKEIQEAYEVLSDPQKRAMYDR 69
PRK14285 PRK14285
chaperone protein DnaJ; Provisional
66-128 8.86e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 172773 [Multi-domain]  Cd Length: 365  Bit Score: 60.01  E-value: 8.86e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15240208   66 DWYGILNASPRDDDETLKRKYRKLALMLHPDKNK-SIGAEGAFKHVSEAWKFLSDKEKRAAYDR 128
Cdd:PRK14285   4 DYYEILGLSKGASKDEIKKAYRKIAIKYHPDKNKgNKEAESIFKEATEAYEVLIDDNKRAQYDR 67
PRK14287 PRK14287
chaperone protein DnaJ; Provisional
66-128 1.80e-09

chaperone protein DnaJ; Provisional


Pssm-ID: 237659 [Multi-domain]  Cd Length: 371  Bit Score: 59.25  E-value: 1.80e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15240208   66 DWYGILNASPRDDDETLKRKYRKLALMLHPDKNKSIGAEGAFKHVSEAWKFLSDKEKRAAYDR 128
Cdd:PRK14287   5 DYYEVLGVDRNASVDEVKKAYRKLARKYHPDVNKAPDAEDKFKEVKEAYDTLSDPQKKAHYDQ 67
PRK14300 PRK14300
chaperone protein DnaJ; Provisional
66-147 2.08e-09

chaperone protein DnaJ; Provisional


Pssm-ID: 172788 [Multi-domain]  Cd Length: 372  Bit Score: 58.87  E-value: 2.08e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240208   66 DWYGILNASPRDDDETLKRKYRKLALMLHPDKNKSIGAEGAFKHVSEAWKFLSDKEKRAAYDRRKSLHSVYQKVSVSSSN 145
Cdd:PRK14300   4 DYYQILGVSKTASQADLKKAYLKLAKQYHPDTTDAKDAEKKFKEINAAYDVLKDEQKRAAYDRFGHDAFQNQQSRGGGGN 83

                 ..
gi 15240208  146 NG 147
Cdd:PRK14300  84 HG 85
PRK14288 PRK14288
molecular chaperone DnaJ;
64-128 2.08e-09

molecular chaperone DnaJ;


Pssm-ID: 172776 [Multi-domain]  Cd Length: 369  Bit Score: 58.93  E-value: 2.08e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15240208   64 DVDWYGILNASPRDDDETLKRKYRKLALMLHPDKNKSIG-AEGAFKHVSEAWKFLSDKEKRAAYDR 128
Cdd:PRK14288   2 ELSYYEILEVEKHSNQETIKKSYRKLALKYHPDRNAGDKeAEEKFKLINEAYGVLSDEKKRALYDR 67
PRK14290 PRK14290
chaperone protein DnaJ; Provisional
66-128 5.34e-08

chaperone protein DnaJ; Provisional


Pssm-ID: 172778 [Multi-domain]  Cd Length: 365  Bit Score: 54.55  E-value: 5.34e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15240208   66 DWYGILNASPRDDDETLKRKYRKLALMLHPDKN--KSIGAEGAFKHVSEAWKFLSDKEKRAAYDR 128
Cdd:PRK14290   4 DYYKILGVDRNASQEDIKKAFRELAKKWHPDLHpgNKAEAEEKFKEISEAYEVLSDPQKRRQYDQ 68
PTZ00037 PTZ00037
DnaJ_C chaperone protein; Provisional
63-127 5.90e-08

DnaJ_C chaperone protein; Provisional


Pssm-ID: 240236 [Multi-domain]  Cd Length: 421  Bit Score: 54.44  E-value: 5.90e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15240208   63 EDVD---WYGILNASPRDDDETLKRKYRKLALMLHPDKNksiGAEGAFKHVSEAWKFLSDKEKRAAYD 127
Cdd:PTZ00037  23 REVDnekLYEVLNLSKDCTTSEIKKAYRKLAIKHHPDKG---GDPEKFKEISRAYEVLSDPEKRKIYD 87
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
66-137 4.81e-06

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


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 44.02  E-value: 4.81e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15240208  66 DWYGILNASPRDDDETLKRKYRKLALMLHPDknksigaegafKHVSEAwkflSDKEKRAAYDRRKSLHSVYQ 137
Cdd:COG1076   5 DAFELLGLPPDADDAELKRAYRKLQREHHPD-----------RLAAGL----PEEEQRLALQKAAAINEAYE 61
djlA PRK09430
co-chaperone DjlA;
66-97 4.46e-03

co-chaperone DjlA;


Pssm-ID: 236512 [Multi-domain]  Cd Length: 267  Bit Score: 38.64  E-value: 4.46e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 15240208   66 DWYGILNASPRDDDETLKRKYRKLALMLHPDK 97
Cdd:PRK09430 201 DAYKVLGVSESDDDQEIKRAYRKLMSEHHPDK 232
ZUO1 COG5269
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ...
51-127 5.06e-03

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


Pssm-ID: 227594 [Multi-domain]  Cd Length: 379  Bit Score: 38.86  E-value: 5.06e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240208  51 LDVYIAAENKVNEDVDWYGILNASP---RDDDETLKRKYRKLALMLHPDKNK---SIGAEGAFKHVSEAWKFLSDKEKRA 124
Cdd:COG5269  29 LNLYTREDFKNWKKVDLYALLGLSKyrtKAIPPQILKAHKKKVYKYHPDKTAaggNKGCDEFFKLIQKAREVLGDRKLRL 108

                ...
gi 15240208 125 AYD 127
Cdd:COG5269 109 QYD 111
 
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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