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Conserved domains on  [gi|61557260|ref|NP_001013214|]
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dnaJ homolog subfamily C member 4 [Rattus norvegicus]

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:  15170475|9644977
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 ...
 31-93 1.30e-26

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: 97.54  E-value: 1.30e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 61557260    31 NYYELLGVHPGASAEEIKRAFFTKSKELHPDRDPGNPALHSRFVELSEAYRVLSREESRRNYD 93
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 ...
 31-93 1.30e-26

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: 97.54  E-value: 1.30e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 61557260    31 NYYELLGVHPGASAEEIKRAFFTKSKELHPDRDPGNPALHSRFVELSEAYRVLSREESRRNYD 93
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNPGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 31-135 5.08e-26

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: 98.62  E-value: 5.08e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557260  31 NYYELLGVHPGASAEEIKRAFFTKSKELHPDRDPGNPALHSRFVELSEAYRVLSREESRRNYDHQLHSASPSKSSGSTAE 110
Cdd:COG0484   1 DYYEILGVSRDASAEEIKKAYRKLAKKYHPDRNPGDPEAEEKFKEINEAYEVLSDPEKRAAYDRFGHAAELLLATELAES 80

                        90       100
                ....*....|....*....|....*
gi 61557260 111 PKYKQQTHSSPWETPNAEYWAQFHS 135
Cdd:COG0484  81 AAAEAAAAEAKEEAAEAGASEYEAI 105
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 31-85 8.56e-20

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: 79.51  E-value: 8.56e-20
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 61557260  31 NYYELLGVHPGASAEEIKRAFFTKSKELHPDRDPGNPALHSRFVELSEAYRVLSR 85
Cdd:cd06257   1 DYYDILGVPPDASDEEIKKAYRKLALKYHPDKNPDDPEAEEKFKEINEAYEVLSD 55
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 31-93 4.88e-19

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 84.43  E-value: 4.88e-19
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 61557260   31 NYYELLGVHPGASAEEIKRAFFTKSKELHPDRDPGNPALHSRFVELSEAYRVLSREESRRNYD 93
Cdd:PRK10767   5 DYYEVLGVSRNASEDEIKKAYRKLAMKYHPDRNPGDKEAEEKFKEIKEAYEVLSDPQKRAAYD 67
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
 32-93 1.95e-18

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: 82.65  E-value: 1.95e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 61557260    32 YYELLGVHPGASAEEIKRAFFTKSKELHPDRDPgNPALHSRFVELSEAYRVLSREESRRNYD 93
Cdd:TIGR02349   2 YYEILGVSKDASEEEIKKAYRKLAKKYHPDRNK-DKEAEEKFKEINEAYEVLSDPEKRAQYD 62
DnaJ smart00271
DnaJ molecular chaperone homology domain;
30-88 7.64e-18

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 74.58  E-value: 7.64e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557260     30 TNYYELLGVHPGASAEEIKRAFFTKSKELHPDRDPGNPAL-HSRFVELSEAYRVLSREES 88
Cdd:smart00271   1 TDYYEILGVPRDASLDEIKKAYRKLALKYHPDKNPGDKEEaEEKFKEINEAYEVLSDPEK 60
terminal_TopJ NF037946
terminal organelle assembly protein TopJ;
31-93 4.46e-15

terminal organelle assembly protein TopJ;


Pssm-ID: 468284 [Multi-domain]  Cd Length: 440  Bit Score: 73.70  E-value: 4.46e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 61557260   31 NYYELLGVHPGASAEEIKRAFFTKSKELHPDRDpGNPALHSRFVELSEAYRVLSREESRRNYD 93
Cdd:NF037946   6 DYYEVLGVDRDADDQEIKKAFRKLAKKYHPDRN-KAPDAAEIFAEINEAYEVLSNPEKRANYD 67
 
Name Accession Description Interval E-value
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 31-93 1.30e-26

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: 97.54  E-value: 1.30e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 61557260    31 NYYELLGVHPGASAEEIKRAFFTKSKELHPDRDPGNPALHSRFVELSEAYRVLSREESRRNYD 93
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNPGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 31-135 5.08e-26

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: 98.62  E-value: 5.08e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557260  31 NYYELLGVHPGASAEEIKRAFFTKSKELHPDRDPGNPALHSRFVELSEAYRVLSREESRRNYDHQLHSASPSKSSGSTAE 110
Cdd:COG0484   1 DYYEILGVSRDASAEEIKKAYRKLAKKYHPDRNPGDPEAEEKFKEINEAYEVLSDPEKRAAYDRFGHAAELLLATELAES 80

                        90       100
                ....*....|....*....|....*
gi 61557260 111 PKYKQQTHSSPWETPNAEYWAQFHS 135
Cdd:COG0484  81 AAAEAAAAEAKEEAAEAGASEYEAI 105
SEC63 COG5407
Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular ...
 31-90 1.31e-20

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


Pssm-ID: 444165 [Multi-domain]  Cd Length: 61  Bit Score: 81.97  E-value: 1.31e-20
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557260  31 NYYELLGVHPGASAEEIKRAFFTKSKELHPDRDPGNPALHSRFVELSEAYRVLSREESRR 90
Cdd:COG5407   1 DPYEVLGVAKTASADEIKKAYRKLAKKYHPDRNKGDPKAEERFKEINEAYELLSDAEKRA 60
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 31-85 8.56e-20

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: 79.51  E-value: 8.56e-20
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 61557260  31 NYYELLGVHPGASAEEIKRAFFTKSKELHPDRDPGNPALHSRFVELSEAYRVLSR 85
Cdd:cd06257   1 DYYDILGVPPDASDEEIKKAYRKLALKYHPDKNPDDPEAEEKFKEINEAYEVLSD 55
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 31-93 4.88e-19

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 84.43  E-value: 4.88e-19
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 61557260   31 NYYELLGVHPGASAEEIKRAFFTKSKELHPDRDPGNPALHSRFVELSEAYRVLSREESRRNYD 93
Cdd:PRK10767   5 DYYEVLGVSRNASEDEIKKAYRKLAMKYHPDRNPGDKEAEEKFKEIKEAYEVLSDPQKRAAYD 67
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
27-96 9.79e-19

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


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 77.84  E-value: 9.79e-19
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 61557260  27 PVPTNYYELLGVHPGASAEEIKRAFFTKSKELHPDRDPGNPAL-HSRFVELSEAYRVLSREESRRNYDHQL 96
Cdd:COG2214   2 PDLKDHYAVLGVPPDASLEEIRQAYRRLAKLLHPDRGGELKALaEELFQRLNEAYEVLSDPERRAEYDREL 72
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
 32-93 1.95e-18

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: 82.65  E-value: 1.95e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 61557260    32 YYELLGVHPGASAEEIKRAFFTKSKELHPDRDPgNPALHSRFVELSEAYRVLSREESRRNYD 93
Cdd:TIGR02349   2 YYEILGVSKDASEEEIKKAYRKLAKKYHPDRNK-DKEAEEKFKEINEAYEVLSDPEKRAQYD 62
DnaJ smart00271
DnaJ molecular chaperone homology domain;
30-88 7.64e-18

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 74.58  E-value: 7.64e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557260     30 TNYYELLGVHPGASAEEIKRAFFTKSKELHPDRDPGNPAL-HSRFVELSEAYRVLSREES 88
Cdd:smart00271   1 TDYYEILGVPRDASLDEIKKAYRKLALKYHPDKNPGDKEEaEEKFKEINEAYEVLSDPEK 60
PRK14279 PRK14279
molecular chaperone DnaJ;
31-93 4.50e-17

molecular chaperone DnaJ;


Pssm-ID: 237655 [Multi-domain]  Cd Length: 392  Bit Score: 79.01  E-value: 4.50e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 61557260   31 NYYELLGVHPGASAEEIKRAFFTKSKELHPDRDPGNPALHSRFVELSEAYRVLSREESRRNYD 93
Cdd:PRK14279  10 DFYKELGVSSDASAEEIKKAYRKLARELHPDANPGDPAAEERFKAVSEAHDVLSDPAKRKEYD 72
PRK14277 PRK14277
chaperone protein DnaJ; Provisional
 31-93 1.04e-16

chaperone protein DnaJ; Provisional


Pssm-ID: 184599 [Multi-domain]  Cd Length: 386  Bit Score: 78.30  E-value: 1.04e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 61557260   31 NYYELLGVHPGASAEEIKRAFFTKSKELHPDRDPGNPALHSRFVELSEAYRVLSREESRRNYD 93
Cdd:PRK14277   6 DYYEILGVDRNATEEEIKKAYRRLAKKYHPDLNPGDKEAEQKFKEINEAYEILSDPQKRAQYD 68
PRK14284 PRK14284
chaperone protein DnaJ; Provisional
 30-93 1.14e-16

chaperone protein DnaJ; Provisional


Pssm-ID: 237658 [Multi-domain]  Cd Length: 391  Bit Score: 77.96  E-value: 1.14e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 61557260   30 TNYYELLGVHPGASAEEIKRAFFTKSKELHPDRDPGNPALHSRFVELSEAYRVLSREESRRNYD 93
Cdd:PRK14284   1 MDYYTILGVSKTASPEEIKKAYRKLAVKYHPDKNPGDAEAEKRFKEVSEAYEVLSDAQKRESYD 64
PRK14301 PRK14301
chaperone protein DnaJ; Provisional
 28-93 3.67e-16

chaperone protein DnaJ; Provisional


Pssm-ID: 237668 [Multi-domain]  Cd Length: 373  Bit Score: 76.32  E-value: 3.67e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 61557260   28 VPTNYYELLGVHPGASAEEIKRAFFTKSKELHPDRDPGNPALHSRFVELSEAYRVLSREESRRNYD 93
Cdd:PRK14301   2 SQRDYYEVLGVSRDASEDEIKKAYRKLALQYHPDRNPDNPEAEQKFKEAAEAYEVLRDAEKRARYD 67
PRK14297 PRK14297
molecular chaperone DnaJ;
31-93 4.62e-16

molecular chaperone DnaJ;


Pssm-ID: 184611 [Multi-domain]  Cd Length: 380  Bit Score: 76.36  E-value: 4.62e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 61557260   31 NYYELLGVHPGASAEEIKRAFFTKSKELHPDRDPGNPALHSRFVELSEAYRVLSREESRRNYD 93
Cdd:PRK14297   5 DYYEVLGLEKGASDDEIKKAFRKLAIKYHPDKNKGNKEAEEKFKEINEAYQVLSDPQKKAQYD 67
terminal_TopJ NF037946
terminal organelle assembly protein TopJ;
31-93 4.46e-15

terminal organelle assembly protein TopJ;


Pssm-ID: 468284 [Multi-domain]  Cd Length: 440  Bit Score: 73.70  E-value: 4.46e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 61557260   31 NYYELLGVHPGASAEEIKRAFFTKSKELHPDRDpGNPALHSRFVELSEAYRVLSREESRRNYD 93
Cdd:NF037946   6 DYYEVLGVDRDADDQEIKKAFRKLAKKYHPDRN-KAPDAAEIFAEINEAYEVLSNPEKRANYD 67
PRK14295 PRK14295
molecular chaperone DnaJ;
31-93 5.09e-15

molecular chaperone DnaJ;


Pssm-ID: 237665 [Multi-domain]  Cd Length: 389  Bit Score: 73.34  E-value: 5.09e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 61557260   31 NYYELLGVHPGASAEEIKRAFFTKSKELHPDRDPGNPALHSRFVELSEAYRVLSREESRRNYD 93
Cdd:PRK14295  10 DYYKVLGVPKDATEAEIKKAYRKLAREYHPDANKGDAKAEERFKEISEAYDVLSDEKKRKEYD 72
PRK14281 PRK14281
chaperone protein DnaJ; Provisional
 31-97 9.03e-15

chaperone protein DnaJ; Provisional


Pssm-ID: 237657 [Multi-domain]  Cd Length: 397  Bit Score: 72.53  E-value: 9.03e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 61557260   31 NYYELLGVHPGASAEEIKRAFFTKSKELHPDRDPGNPALHSRFVELSEAYRVLSREESRRNYDHQLH 97
Cdd:PRK14281   4 DYYEVLGVSRSADKDEIKKAYRKLALKYHPDKNPDNKEAEEHFKEVNEAYEVLSNDDKRRRYDQFGH 70
PRK14289 PRK14289
molecular chaperone DnaJ;
31-97 1.01e-14

molecular chaperone DnaJ;


Pssm-ID: 237660 [Multi-domain]  Cd Length: 386  Bit Score: 72.56  E-value: 1.01e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 61557260   31 NYYELLGVHPGASAEEIKRAFFTKSKELHPDRDPGNPALHSRFVELSEAYRVLSREESRRNYDHQLH 97
Cdd:PRK14289   6 DYYEVLGVSKTATVDEIKKAYRKKAIQYHPDKNPGDKEAEEKFKEAAEAYDVLSDPDKRSRYDQFGH 72
PRK14278 PRK14278
chaperone protein DnaJ; Provisional
 30-93 1.77e-14

chaperone protein DnaJ; Provisional


Pssm-ID: 237654 [Multi-domain]  Cd Length: 378  Bit Score: 71.62  E-value: 1.77e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 61557260   30 TNYYELLGVHPGASAEEIKRAFFTKSKELHPDRDPgNPALHSRFVELSEAYRVLSREESRRNYD 93
Cdd:PRK14278   3 RDYYGLLGVSRNASDAEIKRAYRKLARELHPDVNP-DEEAQEKFKEISVAYEVLSDPEKRRIVD 65
PRK14294 PRK14294
chaperone protein DnaJ; Provisional
 32-97 2.35e-14

chaperone protein DnaJ; Provisional


Pssm-ID: 237664 [Multi-domain]  Cd Length: 366  Bit Score: 71.33  E-value: 2.35e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 61557260   32 YYELLGVHPGASAEEIKRAFFTKSKELHPDRDPGNPALHSRFVELSEAYRVLSREESRRNYDHQLH 97
Cdd:PRK14294   6 YYEILGVTRDASEEEIKKSYRKLAMKYHPDRNPGDKEAEELFKEAAEAYEVLSDPKKRGIYDQYGH 71
PRK14280 PRK14280
molecular chaperone DnaJ;
31-93 5.81e-14

molecular chaperone DnaJ;


Pssm-ID: 237656 [Multi-domain]  Cd Length: 376  Bit Score: 70.14  E-value: 5.81e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 61557260   31 NYYELLGVHPGASAEEIKRAFFTKSKELHPD--RDPGNpalHSRFVELSEAYRVLSREESRRNYD 93
Cdd:PRK14280   5 DYYEVLGVSKSASKDEIKKAYRKLSKKYHPDinKEEGA---DEKFKEISEAYEVLSDDQKRAQYD 66
PRK14282 PRK14282
chaperone protein DnaJ; Provisional
 27-93 5.81e-14

chaperone protein DnaJ; Provisional


Pssm-ID: 184603 [Multi-domain]  Cd Length: 369  Bit Score: 70.21  E-value: 5.81e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 61557260   27 PVPTNYYELLGVHPGASAEEIKRAFFTKSKELHPDRDPGNPAL-HSRFVELSEAYRVLSREESRRNYD 93
Cdd:PRK14282   1 REKKDYYEILGVSRNATQEEIKRAYKRLVKEWHPDRHPENRKEaEQKFKEIQEAYEVLSDPQKRAMYD 68
PRK14290 PRK14290
chaperone protein DnaJ; Provisional
 31-93 7.92e-14

chaperone protein DnaJ; Provisional


Pssm-ID: 172778 [Multi-domain]  Cd Length: 365  Bit Score: 69.57  E-value: 7.92e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 61557260   31 NYYELLGVHPGASAEEIKRAFFTKSKELHPDRDPGNPA-LHSRFVELSEAYRVLSREESRRNYD 93
Cdd:PRK14290   4 DYYKILGVDRNASQEDIKKAFRELAKKWHPDLHPGNKAeAEEKFKEISEAYEVLSDPQKRRQYD 67
PRK14291 PRK14291
chaperone protein DnaJ; Provisional
 31-97 9.61e-14

chaperone protein DnaJ; Provisional


Pssm-ID: 237661 [Multi-domain]  Cd Length: 382  Bit Score: 69.41  E-value: 9.61e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 61557260   31 NYYELLGVHPGASAEEIKRAFFTKSKELHPDRDPgNPALHSRFVELSEAYRVLSREESRRNYDHQLH 97
Cdd:PRK14291   4 DYYEILGVSRNATQEEIKKAYRRLARKYHPDFNK-NPEAEEKFKEINEAYQVLSDPEKRKLYDQFGH 69
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
 31-93 8.62e-13

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 66.80  E-value: 8.62e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 61557260   31 NYYELLGVHPGASAEEIKRAFFTKSKELHPDRDPgNPALHSRFVELSEAYRVLSREESRRNYD 93
Cdd:PRK14298   6 DYYEILGLSKDASVEDIKKAYRKLAMKYHPDKNK-EPDAEEKFKEISEAYAVLSDAEKRAQYD 67
PRK14293 PRK14293
molecular chaperone DnaJ;
29-93 1.38e-12

molecular chaperone DnaJ;


Pssm-ID: 237663 [Multi-domain]  Cd Length: 374  Bit Score: 66.17  E-value: 1.38e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 61557260   29 PTNYYELLGVHPGASAEEIKRAFFTKSKELHPD--RDPGNpalHSRFVELSEAYRVLSREESRRNYD 93
Cdd:PRK14293   2 AADYYEILGVSRDADKDELKRAYRRLARKYHPDvnKEPGA---EDRFKEINRAYEVLSDPETRARYD 65
PRK14292 PRK14292
chaperone protein DnaJ; Provisional
 31-93 2.52e-12

chaperone protein DnaJ; Provisional


Pssm-ID: 237662 [Multi-domain]  Cd Length: 371  Bit Score: 65.30  E-value: 2.52e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 61557260   31 NYYELLGVHPGASAEEIKRAFFTKSKELHPDRDPgNPALHSRFVELSEAYRVLSREESRRNYD 93
Cdd:PRK14292   3 DYYELLGVSRTASADEIKSAYRKLALKYHPDRNK-EKGAAEKFAQINEAYAVLSDAEKRAHYD 64
PRK14285 PRK14285
chaperone protein DnaJ; Provisional
 31-97 1.01e-11

chaperone protein DnaJ; Provisional


Pssm-ID: 172773 [Multi-domain]  Cd Length: 365  Bit Score: 63.47  E-value: 1.01e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 61557260   31 NYYELLGVHPGASAEEIKRAFFTKSKELHPDRDPGNPALHSRFVELSEAYRVLSREESRRNYDHQLH 97
Cdd:PRK14285   4 DYYEILGLSKGASKDEIKKAYRKIAIKYHPDKNKGNKEAESIFKEATEAYEVLIDDNKRAQYDRFGH 70
PRK14283 PRK14283
chaperone protein DnaJ; Provisional
 31-97 1.04e-11

chaperone protein DnaJ; Provisional


Pssm-ID: 184604 [Multi-domain]  Cd Length: 378  Bit Score: 63.69  E-value: 1.04e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 61557260   31 NYYELLGVHPGASAEEIKRAFFTKSKELHPDRDPgNPALHSRFVELSEAYRVLSREESRRNYDHQLH 97
Cdd:PRK14283   6 DYYEVLGVDRNADKKEIKKAYRKLARKYHPDVSE-EEGAEEKFKEISEAYAVLSDDEKRQRYDQFGH 71
PRK14286 PRK14286
chaperone protein DnaJ; Provisional
 32-94 1.92e-11

chaperone protein DnaJ; Provisional


Pssm-ID: 172774 [Multi-domain]  Cd Length: 372  Bit Score: 62.70  E-value: 1.92e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 61557260   32 YYELLGVHPGASAEEIKRAFFTKSKELHPDRDPGNPALHSRFVELSEAYRVLSREESRRNYDH 94
Cdd:PRK14286   6 YYDILGVSKSANDEEIKSAYRKLAIKYHPDKNKGNKESEEKFKEATEAYEILRDPKKRQAYDQ 68
PRK14276 PRK14276
chaperone protein DnaJ; Provisional
 30-93 2.26e-11

chaperone protein DnaJ; Provisional


Pssm-ID: 237653 [Multi-domain]  Cd Length: 380  Bit Score: 62.41  E-value: 2.26e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 61557260   30 TNYYELLGVHPGASAEEIKRAFFTKSKELHPD--RDPGnpaLHSRFVELSEAYRVLSREESRRNYD 93
Cdd:PRK14276   4 TEYYDRLGVSKDASQDEIKKAYRKLSKKYHPDinKEPG---AEEKYKEVQEAYETLSDPQKRAAYD 66
termin_org_DnaJ TIGR03835
terminal organelle assembly protein TopJ; This model describes TopJ (MG_200, CbpA), a DnaJ ...
 31-97 2.45e-11

terminal organelle assembly protein TopJ; This model describes TopJ (MG_200, CbpA), a DnaJ homolog and probable assembly protein of the Mycoplasma terminal organelle. The terminal organelle is involved in both cytadherence and gliding motility. [Cellular processes, Chemotaxis and motility]


Pssm-ID: 274808 [Multi-domain]  Cd Length: 871  Bit Score: 62.91  E-value: 2.45e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 61557260    31 NYYELLGVHPGASAEEIKRAFFTKSKELHPDRDpGNPALHSRFVELSEAYRVLSREESRRNYDHQLH 97
Cdd:TIGR03835   3 DYYEVLGIDRDADEQEIKKAFRKLAKKYHPDRN-KAPDAASIFAEINEANDVLSNPKKRANYDKYGH 68
PRK14299 PRK14299
chaperone protein DnaJ; Provisional
 31-93 3.52e-11

chaperone protein DnaJ; Provisional


Pssm-ID: 237667 [Multi-domain]  Cd Length: 291  Bit Score: 61.49  E-value: 3.52e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 61557260   31 NYYELLGVHPGASAEEIKRAFFTKSKELHPDRDPgNPALHSRFVELSEAYRVLSREESRRNYD 93
Cdd:PRK14299   5 DYYAILGVPKNASQDEIKKAFKKLARKYHPDVNK-SPGAEEKFKEINEAYTVLSDPEKRRIYD 66
PRK10266 PRK10266
curved DNA-binding protein;
31-148 4.09e-11

curved DNA-binding protein;


Pssm-ID: 182347 [Multi-domain]  Cd Length: 306  Bit Score: 61.38  E-value: 4.09e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557260   31 NYYELLGVHPGASAEEIKRAFFTKSKELHPDRDPGNPAlHSRFVELSEAYRVLSREESRRNYDH-QLHSAspskssgsta 109
Cdd:PRK10266   5 DYYAIMGVKPTDDLKTIKTAYRRLARKYHPDVSKEPDA-EARFKEVAEAWEVLSDEQRRAEYDQlWQHRN---------- 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 61557260  110 EPKYKQQTHSSPWETPNAEYWAQ-FHSVRPQEPESRKQQH 148
Cdd:PRK10266  74 DPQFNRQFQHGDGQSFNAEDFDDiFSSIFGQHARQSRQRP 113
PRK14296 PRK14296
chaperone protein DnaJ; Provisional
 31-97 4.37e-09

chaperone protein DnaJ; Provisional


Pssm-ID: 237666 [Multi-domain]  Cd Length: 372  Bit Score: 55.72  E-value: 4.37e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 61557260   31 NYYELLGVHPGASAEEIKRAFFTKSKELHPDRDPgNPALHSRFVELSEAYRVLSREESRRNYDHQLH 97
Cdd:PRK14296   5 DYYEVLGVSKTASEQEIRQAYRKLAKQYHPDLNK-SPDAHDKMVEINEAADVLLDKDKRKQYDQFGH 70
PRK14300 PRK14300
chaperone protein DnaJ; Provisional
 31-97 1.27e-08

chaperone protein DnaJ; Provisional


Pssm-ID: 172788 [Multi-domain]  Cd Length: 372  Bit Score: 54.64  E-value: 1.27e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 61557260   31 NYYELLGVHPGASAEEIKRAFFTKSKELHPDRDPGNPAlHSRFVELSEAYRVLSREESRRNYDHQLH 97
Cdd:PRK14300   4 DYYQILGVSKTASQADLKKAYLKLAKQYHPDTTDAKDA-EKKFKEINAAYDVLKDEQKRAAYDRFGH 69
PTZ00037 PTZ00037
DnaJ_C chaperone protein; Provisional
 26-93 1.70e-08

DnaJ_C chaperone protein; Provisional


Pssm-ID: 240236 [Multi-domain]  Cd Length: 421  Bit Score: 54.06  E-value: 1.70e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 61557260   26 RPVPTN-YYELLGVHPGASAEEIKRAFFTKSKELHPDRDpGNPalhSRFVELSEAYRVLSREESRRNYD 93
Cdd:PTZ00037  23 REVDNEkLYEVLNLSKDCTTSEIKKAYRKLAIKHHPDKG-GDP---EKFKEISRAYEVLSDPEKRKIYD 87
PRK14287 PRK14287
chaperone protein DnaJ; Provisional
 31-97 1.92e-08

chaperone protein DnaJ; Provisional


Pssm-ID: 237659 [Multi-domain]  Cd Length: 371  Bit Score: 53.86  E-value: 1.92e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 61557260   31 NYYELLGVHPGASAEEIKRAFFTKSKELHPDRDPGnPALHSRFVELSEAYRVLSREESRRNYDHQLH 97
Cdd:PRK14287   5 DYYEVLGVDRNASVDEVKKAYRKLARKYHPDVNKA-PDAEDKFKEVKEAYDTLSDPQKKAHYDQFGH 70
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
31-86 1.22e-07

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


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 47.87  E-value: 1.22e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 61557260  31 NYYELLGVHPGASAEEIKRAFFTKSKELHPDR--DPGNPALH----SRFVELSEAYRVLSRE 86
Cdd:COG1076   5 DAFELLGLPPDADDAELKRAYRKLQREHHPDRlaAGLPEEEQrlalQKAAAINEAYETLKDP 66
PRK14288 PRK14288
molecular chaperone DnaJ;
31-93 3.13e-07

molecular chaperone DnaJ;


Pssm-ID: 172776 [Multi-domain]  Cd Length: 369  Bit Score: 50.46  E-value: 3.13e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 61557260   31 NYYELLGVHPGASAEEIKRAFFTKSKELHPDRDPGNPALHSRFVELSEAYRVLSREESRRNYD 93
Cdd:PRK14288   4 SYYEILEVEKHSNQETIKKSYRKLALKYHPDRNAGDKEAEEKFKLINEAYGVLSDEKKRALYD 66
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
 28-93 4.07e-07

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 50.56  E-value: 4.07e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 61557260    28 VP-TNYYELLGVHPGASAEEIKRAFFTKSKELHPDRDPGNPALHsRFVELSEAYRVLSREESRRNYD 93
Cdd:PTZ00341  570 IPdTLFYDILGVGVNADMKEISERYFKLAENYYPPKRSGNEGFH-KFKKINEAYQILGDIDKKKMYN 635
 
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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