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Conserved domains on  [gi|18409985|ref|NP_565034|]
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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
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 ...
 39-88 8.32e-19

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: 74.05  E-value: 8.32e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 18409985    39 SHYTVLGLTPLASQTEVKRAFKRLALKYHPDVHKGQ---DKDFKEIKSAYECL 88
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNPGDpeaEEKFKEINEAYEVL 53
 
Name Accession Description Interval E-value
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 39-88 8.32e-19

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: 74.05  E-value: 8.32e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 18409985    39 SHYTVLGLTPLASQTEVKRAFKRLALKYHPDVHKGQ---DKDFKEIKSAYECL 88
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNPGDpeaEEKFKEINEAYEVL 53
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 39-88 8.14e-18

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: 73.58  E-value: 8.14e-18
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 18409985  39 SHYTVLGLTPLASQTEVKRAFKRLALKYHPDVHKGqDKD----FKEIKSAYECL 88
Cdd:COG0484   1 DYYEILGVSRDASAEEIKKAYRKLAKKYHPDRNPG-DPEaeekFKEINEAYEVL 53
DnaJ smart00271
DnaJ molecular chaperone homology domain;
39-88 1.00e-17

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 71.11  E-value: 1.00e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 18409985     39 SHYTVLGLTPLASQTEVKRAFKRLALKYHPDVHKGQDKD----FKEIKSAYECL 88
Cdd:smart00271   2 DYYEILGVPRDASLDEIKKAYRKLALKYHPDKNPGDKEEaeekFKEINEAYEVL 55
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 40-88 4.03e-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: 66.80  E-value: 4.03e-16
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 18409985  40 HYTVLGLTPLASQTEVKRAFKRLALKYHPDVHKGQ---DKDFKEIKSAYECL 88
Cdd:cd06257   2 YYDILGVPPDASDEEIKKAYRKLALKYHPDKNPDDpeaEEKFKEINEAYEVL 53
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 41-88 1.68e-15

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 70.94  E-value: 1.68e-15
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 18409985   41 YTVLGLTPLASQTEVKRAFKRLALKYHPDVHKGqDKD----FKEIKSAYECL 88
Cdd:PRK10767   7 YEVLGVSRNASEDEIKKAYRKLAMKYHPDRNPG-DKEaeekFKEIKEAYEVL 57
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
 41-88 1.67e-14

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: 68.01  E-value: 1.67e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 18409985    41 YTVLGLTPLASQTEVKRAFKRLALKYHPDVHKgqDKD----FKEIKSAYECL 88
Cdd:TIGR02349   3 YEILGVSKDASEEEIKKAYRKLAKKYHPDRNK--DKEaeekFKEINEAYEVL 52
 
Name Accession Description Interval E-value
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 39-88 8.32e-19

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: 74.05  E-value: 8.32e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 18409985    39 SHYTVLGLTPLASQTEVKRAFKRLALKYHPDVHKGQ---DKDFKEIKSAYECL 88
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNPGDpeaEEKFKEINEAYEVL 53
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 39-88 8.14e-18

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: 73.58  E-value: 8.14e-18
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 18409985  39 SHYTVLGLTPLASQTEVKRAFKRLALKYHPDVHKGqDKD----FKEIKSAYECL 88
Cdd:COG0484   1 DYYEILGVSRDASAEEIKKAYRKLAKKYHPDRNPG-DPEaeekFKEINEAYEVL 53
DnaJ smart00271
DnaJ molecular chaperone homology domain;
39-88 1.00e-17

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 71.11  E-value: 1.00e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 18409985     39 SHYTVLGLTPLASQTEVKRAFKRLALKYHPDVHKGQDKD----FKEIKSAYECL 88
Cdd:smart00271   2 DYYEILGVPRDASLDEIKKAYRKLALKYHPDKNPGDKEEaeekFKEINEAYEVL 55
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 40-88 4.03e-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: 66.80  E-value: 4.03e-16
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 18409985  40 HYTVLGLTPLASQTEVKRAFKRLALKYHPDVHKGQ---DKDFKEIKSAYECL 88
Cdd:cd06257   2 YYDILGVPPDASDEEIKKAYRKLALKYHPDKNPDDpeaEEKFKEINEAYEVL 53
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 41-88 1.68e-15

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 70.94  E-value: 1.68e-15
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 18409985   41 YTVLGLTPLASQTEVKRAFKRLALKYHPDVHKGqDKD----FKEIKSAYECL 88
Cdd:PRK10767   7 YEVLGVSRNASEDEIKKAYRKLAMKYHPDRNPG-DKEaeekFKEIKEAYEVL 57
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
 41-88 1.67e-14

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: 68.01  E-value: 1.67e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 18409985    41 YTVLGLTPLASQTEVKRAFKRLALKYHPDVHKgqDKD----FKEIKSAYECL 88
Cdd:TIGR02349   3 YEILGVSKDASEEEIKKAYRKLAKKYHPDRNK--DKEaeekFKEINEAYEVL 52
PRK14280 PRK14280
molecular chaperone DnaJ;
40-88 1.69e-14

molecular chaperone DnaJ;


Pssm-ID: 237656 [Multi-domain]  Cd Length: 376  Bit Score: 68.21  E-value: 1.69e-14
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 18409985   40 HYTVLGLTPLASQTEVKRAFKRLALKYHPDVHK--GQDKDFKEIKSAYECL 88
Cdd:PRK14280   6 YYEVLGVSKSASKDEIKKAYRKLSKKYHPDINKeeGADEKFKEISEAYEVL 56
PRK14299 PRK14299
chaperone protein DnaJ; Provisional
 40-88 1.27e-13

chaperone protein DnaJ; Provisional


Pssm-ID: 237667 [Multi-domain]  Cd Length: 291  Bit Score: 65.35  E-value: 1.27e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 18409985   40 HYTVLGLTPLASQTEVKRAFKRLALKYHPDVHK--GQDKDFKEIKSAYECL 88
Cdd:PRK14299   6 YYAILGVPKNASQDEIKKAFKKLARKYHPDVNKspGAEEKFKEINEAYTVL 56
PRK14293 PRK14293
molecular chaperone DnaJ;
41-88 7.37e-13

molecular chaperone DnaJ;


Pssm-ID: 237663 [Multi-domain]  Cd Length: 374  Bit Score: 63.47  E-value: 7.37e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 18409985   41 YTVLGLTPLASQTEVKRAFKRLALKYHPDVHK--GQDKDFKEIKSAYECL 88
Cdd:PRK14293   6 YEILGVSRDADKDELKRAYRRLARKYHPDVNKepGAEDRFKEINRAYEVL 55
PRK14276 PRK14276
chaperone protein DnaJ; Provisional
 41-88 1.16e-12

chaperone protein DnaJ; Provisional


Pssm-ID: 237653 [Multi-domain]  Cd Length: 380  Bit Score: 62.80  E-value: 1.16e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 18409985   41 YTVLGLTPLASQTEVKRAFKRLALKYHPDVHK--GQDKDFKEIKSAYECL 88
Cdd:PRK14276   7 YDRLGVSKDASQDEIKKAYRKLSKKYHPDINKepGAEEKYKEVQEAYETL 56
PRK14297 PRK14297
molecular chaperone DnaJ;
40-88 1.33e-12

molecular chaperone DnaJ;


Pssm-ID: 184611 [Multi-domain]  Cd Length: 380  Bit Score: 62.88  E-value: 1.33e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 18409985   40 HYTVLGLTPLASQTEVKRAFKRLALKYHPDVHKGQ---DKDFKEIKSAYECL 88
Cdd:PRK14297   6 YYEVLGLEKGASDDEIKKAFRKLAIKYHPDKNKGNkeaEEKFKEINEAYQVL 57
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
39-88 1.44e-12

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


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 58.96  E-value: 1.44e-12
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 18409985  39 SHYTVLGLTPLASQTEVKRAFKRLALKYHPDVHKGQDKD----FKEIKSAYECL 88
Cdd:COG2214   6 DHYAVLGVPPDASLEEIRQAYRRLAKLLHPDRGGELKALaeelFQRLNEAYEVL 59
PRK14278 PRK14278
chaperone protein DnaJ; Provisional
 40-88 3.08e-12

chaperone protein DnaJ; Provisional


Pssm-ID: 237654 [Multi-domain]  Cd Length: 378  Bit Score: 61.61  E-value: 3.08e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 18409985   40 HYTVLGLTPLASQTEVKRAFKRLALKYHPDVH---KGQDKdFKEIKSAYECL 88
Cdd:PRK14278   5 YYGLLGVSRNASDAEIKRAYRKLARELHPDVNpdeEAQEK-FKEISVAYEVL 55
PRK14277 PRK14277
chaperone protein DnaJ; Provisional
 40-88 5.66e-12

chaperone protein DnaJ; Provisional


Pssm-ID: 184599 [Multi-domain]  Cd Length: 386  Bit Score: 60.97  E-value: 5.66e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 18409985   40 HYTVLGLTPLASQTEVKRAFKRLALKYHPDVHKGQ---DKDFKEIKSAYECL 88
Cdd:PRK14277   7 YYEILGVDRNATEEEIKKAYRRLAKKYHPDLNPGDkeaEQKFKEINEAYEIL 58
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
 40-88 9.81e-12

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 60.25  E-value: 9.81e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 18409985   40 HYTVLGLTPLASQTEVKRAFKRLALKYHPDVHK--GQDKDFKEIKSAYECL 88
Cdd:PRK14298   7 YYEILGLSKDASVEDIKKAYRKLAMKYHPDKNKepDAEEKFKEISEAYAVL 57
PRK14291 PRK14291
chaperone protein DnaJ; Provisional
 40-88 2.39e-11

chaperone protein DnaJ; Provisional


Pssm-ID: 237661 [Multi-domain]  Cd Length: 382  Bit Score: 59.40  E-value: 2.39e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 18409985   40 HYTVLGLTPLASQTEVKRAFKRLALKYHPDVHK--GQDKDFKEIKSAYECL 88
Cdd:PRK14291   5 YYEILGVSRNATQEEIKKAYRRLARKYHPDFNKnpEAEEKFKEINEAYQVL 55
PRK14287 PRK14287
chaperone protein DnaJ; Provisional
 40-88 3.41e-11

chaperone protein DnaJ; Provisional


Pssm-ID: 237659 [Multi-domain]  Cd Length: 371  Bit Score: 58.87  E-value: 3.41e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 18409985   40 HYTVLGLTPLASQTEVKRAFKRLALKYHPDVHKGQDKD--FKEIKSAYECL 88
Cdd:PRK14287   6 YYEVLGVDRNASVDEVKKAYRKLARKYHPDVNKAPDAEdkFKEVKEAYDTL 56
PRK14286 PRK14286
chaperone protein DnaJ; Provisional
 37-88 3.53e-11

chaperone protein DnaJ; Provisional


Pssm-ID: 172774 [Multi-domain]  Cd Length: 372  Bit Score: 58.85  E-value: 3.53e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 18409985   37 DLSHYTVLGLTPLASQTEVKRAFKRLALKYHPDVHKGQ---DKDFKEIKSAYECL 88
Cdd:PRK14286   3 ERSYYDILGVSKSANDEEIKSAYRKLAIKYHPDKNKGNkesEEKFKEATEAYEIL 57
PRK14282 PRK14282
chaperone protein DnaJ; Provisional
 40-88 5.19e-11

chaperone protein DnaJ; Provisional


Pssm-ID: 184603 [Multi-domain]  Cd Length: 369  Bit Score: 58.27  E-value: 5.19e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 18409985   40 HYTVLGLTPLASQTEVKRAFKRLALKYHPDVHKGQDKD----FKEIKSAYECL 88
Cdd:PRK14282   6 YYEILGVSRNATQEEIKRAYKRLVKEWHPDRHPENRKEaeqkFKEIQEAYEVL 58
PRK14284 PRK14284
chaperone protein DnaJ; Provisional
 40-88 6.04e-11

chaperone protein DnaJ; Provisional


Pssm-ID: 237658 [Multi-domain]  Cd Length: 391  Bit Score: 58.32  E-value: 6.04e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 18409985   40 HYTVLGLTPLASQTEVKRAFKRLALKYHPDVHKGQ---DKDFKEIKSAYECL 88
Cdd:PRK14284   3 YYTILGVSKTASPEEIKKAYRKLAVKYHPDKNPGDaeaEKRFKEVSEAYEVL 54
PRK14281 PRK14281
chaperone protein DnaJ; Provisional
 40-88 1.23e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 237657 [Multi-domain]  Cd Length: 397  Bit Score: 57.13  E-value: 1.23e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 18409985   40 HYTVLGLTPLASQTEVKRAFKRLALKYHPDVHKGqDKD----FKEIKSAYECL 88
Cdd:PRK14281   5 YYEVLGVSRSADKDEIKKAYRKLALKYHPDKNPD-NKEaeehFKEVNEAYEVL 56
PRK14283 PRK14283
chaperone protein DnaJ; Provisional
 40-88 1.78e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 184604 [Multi-domain]  Cd Length: 378  Bit Score: 56.76  E-value: 1.78e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 18409985   40 HYTVLGLTPLASQTEVKRAFKRLALKYHPDV--HKGQDKDFKEIKSAYECL 88
Cdd:PRK14283   7 YYEVLGVDRNADKKEIKKAYRKLARKYHPDVseEEGAEEKFKEISEAYAVL 57
PRK14290 PRK14290
chaperone protein DnaJ; Provisional
 40-88 1.85e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 172778 [Multi-domain]  Cd Length: 365  Bit Score: 56.86  E-value: 1.85e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 18409985   40 HYTVLGLTPLASQTEVKRAFKRLALKYHPDVHKGQ----DKDFKEIKSAYECL 88
Cdd:PRK14290   5 YYKILGVDRNASQEDIKKAFRELAKKWHPDLHPGNkaeaEEKFKEISEAYEVL 57
PTZ00037 PTZ00037
DnaJ_C chaperone protein; Provisional
 41-88 2.30e-10

DnaJ_C chaperone protein; Provisional


Pssm-ID: 240236 [Multi-domain]  Cd Length: 421  Bit Score: 56.37  E-value: 2.30e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 18409985   41 YTVLGLTPLASQTEVKRAFKRLALKYHPDvhKGQDKD-FKEIKSAYECL 88
Cdd:PTZ00037  31 YEVLNLSKDCTTSEIKKAYRKLAIKHHPD--KGGDPEkFKEISRAYEVL 77
PRK10266 PRK10266
curved DNA-binding protein;
40-88 2.49e-10

curved DNA-binding protein;


Pssm-ID: 182347 [Multi-domain]  Cd Length: 306  Bit Score: 56.37  E-value: 2.49e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 18409985   40 HYTVLGLTPLASQTEVKRAFKRLALKYHPDVHKGQDKD--FKEIKSAYECL 88
Cdd:PRK10266   6 YYAIMGVKPTDDLKTIKTAYRRLARKYHPDVSKEPDAEarFKEVAEAWEVL 56
PRK14295 PRK14295
molecular chaperone DnaJ;
40-88 2.63e-10

molecular chaperone DnaJ;


Pssm-ID: 237665 [Multi-domain]  Cd Length: 389  Bit Score: 56.40  E-value: 2.63e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 18409985   40 HYTVLGLTPLASQTEVKRAFKRLALKYHPDVHKGQ---DKDFKEIKSAYECL 88
Cdd:PRK14295  11 YYKVLGVPKDATEAEIKKAYRKLAREYHPDANKGDakaEERFKEISEAYDVL 62
PRK14300 PRK14300
chaperone protein DnaJ; Provisional
 40-88 5.98e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 172788 [Multi-domain]  Cd Length: 372  Bit Score: 55.41  E-value: 5.98e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 18409985   40 HYTVLGLTPLASQTEVKRAFKRLALKYHPDVHKGQD--KDFKEIKSAYECL 88
Cdd:PRK14300   5 YYQILGVSKTASQADLKKAYLKLAKQYHPDTTDAKDaeKKFKEINAAYDVL 55
PRK14285 PRK14285
chaperone protein DnaJ; Provisional
 40-88 6.91e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 172773 [Multi-domain]  Cd Length: 365  Bit Score: 55.00  E-value: 6.91e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 18409985   40 HYTVLGLTPLASQTEVKRAFKRLALKYHPDVHKGQDKD---FKEIKSAYECL 88
Cdd:PRK14285   5 YYEILGLSKGASKDEIKKAYRKIAIKYHPDKNKGNKEAesiFKEATEAYEVL 56
PRK14294 PRK14294
chaperone protein DnaJ; Provisional
 40-88 1.69e-09

chaperone protein DnaJ; Provisional


Pssm-ID: 237664 [Multi-domain]  Cd Length: 366  Bit Score: 54.00  E-value: 1.69e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 18409985   40 HYTVLGLTPLASQTEVKRAFKRLALKYHPDVHKGqDKD----FKEIKSAYECL 88
Cdd:PRK14294   6 YYEILGVTRDASEEEIKKSYRKLAMKYHPDRNPG-DKEaeelFKEAAEAYEVL 57
djlA PRK09430
co-chaperone DjlA;
41-86 1.22e-08

co-chaperone DjlA;


Pssm-ID: 236512 [Multi-domain]  Cd Length: 267  Bit Score: 51.35  E-value: 1.22e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 18409985   41 YTVLGLTPLASQTEVKRAFKRLALKYHPD--VHKGQDKDF--------KEIKSAYE 86
Cdd:PRK09430 203 YKVLGVSESDDDQEIKRAYRKLMSEHHPDklVAKGLPPEMmemakekaQEIQAAYE 258
PRK14301 PRK14301
chaperone protein DnaJ; Provisional
 40-88 1.32e-08

chaperone protein DnaJ; Provisional


Pssm-ID: 237668 [Multi-domain]  Cd Length: 373  Bit Score: 51.28  E-value: 1.32e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 18409985   40 HYTVLGLTPLASQTEVKRAFKRLALKYHPDVHKGQ---DKDFKEIKSAYECL 88
Cdd:PRK14301   6 YYEVLGVSRDASEDEIKKAYRKLALQYHPDRNPDNpeaEQKFKEAAEAYEVL 57
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
40-88 1.37e-08

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


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 48.25  E-value: 1.37e-08
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 18409985  40 HYTVLGLTPLASQTEVKRAFKRLALKYHPDVH-KGQDKDFK--------EIKSAYECL 88
Cdd:COG1076   6 AFELLGLPPDADDAELKRAYRKLQREHHPDRLaAGLPEEEQrlalqkaaAINEAYETL 63
PRK14292 PRK14292
chaperone protein DnaJ; Provisional
 38-88 4.05e-08

chaperone protein DnaJ; Provisional


Pssm-ID: 237662 [Multi-domain]  Cd Length: 371  Bit Score: 49.89  E-value: 4.05e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 18409985   38 LSHYTVLGLTPLASQTEVKRAFKRLALKYHPDVHK--GQDKDFKEIKSAYECL 88
Cdd:PRK14292   2 MDYYELLGVSRTASADEIKSAYRKLALKYHPDRNKekGAAEKFAQINEAYAVL 54
PRK14296 PRK14296
chaperone protein DnaJ; Provisional
 40-88 4.86e-08

chaperone protein DnaJ; Provisional


Pssm-ID: 237666 [Multi-domain]  Cd Length: 372  Bit Score: 49.95  E-value: 4.86e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 18409985   40 HYTVLGLTPLASQTEVKRAFKRLALKYHPDVHK--GQDKDFKEIKSAYECL 88
Cdd:PRK14296   6 YYEVLGVSKTASEQEIRQAYRKLAKQYHPDLNKspDAHDKMVEINEAADVL 56
PRK14288 PRK14288
molecular chaperone DnaJ;
37-88 5.46e-06

molecular chaperone DnaJ;


Pssm-ID: 172776 [Multi-domain]  Cd Length: 369  Bit Score: 43.91  E-value: 5.46e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 18409985   37 DLSHYTVLGLTPLASQTEVKRAFKRLALKYHPDVHKGQ---DKDFKEIKSAYECL 88
Cdd:PRK14288   2 ELSYYEILEVEKHSNQETIKKSYRKLALKYHPDRNAGDkeaEEKFKLINEAYGVL 56
ZUO1 COG5269
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ...
 40-88 1.89e-05

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


Pssm-ID: 227594 [Multi-domain]  Cd Length: 379  Bit Score: 42.33  E-value: 1.89e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 18409985  40 HYTVLGLTPL---ASQTEVKRAFKRLALKYHPDV-----HKGQDKDFKEIKSAYECL 88
Cdd:COG5269  45 LYALLGLSKYrtkAIPPQILKAHKKKVYKYHPDKtaaggNKGCDEFFKLIQKAREVL 101
 
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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