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Conserved domains on  [gi|1503143914|ref|XP_026806719|]
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dnaJ homolog subfamily B member 6-like isoform X1 [Rhopalosiphum maidis]

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 ...
 4-67 2.32e-32

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: 113.34  E-value: 2.32e-32
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1503143914   4 DYYSILEVTPNASINDIKKSYRKLALKWHPDKNPENQEqANRMFKEISEAYEVLSDEAKRKLYD 67
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNPGDPE-AEEKFKEINEAYEVLSDPEKRAIYD 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 ...
 4-67 2.32e-32

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: 113.34  E-value: 2.32e-32
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1503143914   4 DYYSILEVTPNASINDIKKSYRKLALKWHPDKNPENQEqANRMFKEISEAYEVLSDEAKRKLYD 67
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNPGDPE-AEEKFKEINEAYEVLSDPEKRAIYD 63
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 4-68 1.71e-30

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: 111.33  E-value: 1.71e-30
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1503143914   4 DYYSILEVTPNASINDIKKSYRKLALKWHPDKNPENQEqANRMFKEISEAYEVLSDEAKRKLYDE 68
Cdd:COG0484     1 DYYEILGVSRDASAEEIKKAYRKLAKKYHPDRNPGDPE-AEEKFKEINEAYEVLSDPEKRAAYDR 64
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 4-67 1.49e-29

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 114.47  E-value: 1.49e-29
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1503143914   4 DYYSILEVTPNASINDIKKSYRKLALKWHPDKNPENQEqANRMFKEISEAYEVLSDEAKRKLYD 67
Cdd:PRK10767    5 DYYEVLGVSRNASEDEIKKAYRKLAMKYHPDRNPGDKE-AEEKFKEIKEAYEVLSDPQKRAAYD 67
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
 4-68 1.02e-27

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: 109.23  E-value: 1.02e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1503143914   4 DYYSILEVTPNASINDIKKSYRKLALKWHPDKNPEnqEQANRMFKEISEAYEVLSDEAKRKLYDE 68
Cdd:TIGR02349   1 DYYEILGVSKDASEEEIKKAYRKLAKKYHPDRNKD--KEAEEKFKEINEAYEVLSDPEKRAQYDQ 63
DnaJ smart00271
DnaJ molecular chaperone homology domain;
4-62 4.11e-27

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 99.62  E-value: 4.11e-27
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1503143914    4 DYYSILEVTPNASINDIKKSYRKLALKWHPDKNPENQEQANRMFKEISEAYEVLSDEAK 62
Cdd:smart00271   2 DYYEILGVPRDASLDEIKKAYRKLALKYHPDKNPGDKEEAEEKFKEINEAYEVLSDPEK 60
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 4-59 1.32e-24

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: 92.99  E-value: 1.32e-24
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1503143914   4 DYYSILEVTPNASINDIKKSYRKLALKWHPDKNPENqEQANRMFKEISEAYEVLSD 59
Cdd:cd06257     1 DYYDILGVPPDASDEEIKKAYRKLALKYHPDKNPDD-PEAEEKFKEINEAYEVLSD 55
terminal_TopJ NF037946
terminal organelle assembly protein TopJ;
4-67 1.02e-18

terminal organelle assembly protein TopJ;


Pssm-ID: 468284 [Multi-domain]  Cd Length: 440  Bit Score: 85.26  E-value: 1.02e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1503143914   4 DYYSILEVTPNASINDIKKSYRKLALKWHPDKNpeNQEQANRMFKEISEAYEVLSDEAKRKLYD 67
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 ...
 4-67 2.32e-32

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: 113.34  E-value: 2.32e-32
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1503143914   4 DYYSILEVTPNASINDIKKSYRKLALKWHPDKNPENQEqANRMFKEISEAYEVLSDEAKRKLYD 67
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNPGDPE-AEEKFKEINEAYEVLSDPEKRAIYD 63
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 4-68 1.71e-30

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: 111.33  E-value: 1.71e-30
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1503143914   4 DYYSILEVTPNASINDIKKSYRKLALKWHPDKNPENQEqANRMFKEISEAYEVLSDEAKRKLYDE 68
Cdd:COG0484     1 DYYEILGVSRDASAEEIKKAYRKLAKKYHPDRNPGDPE-AEEKFKEINEAYEVLSDPEKRAAYDR 64
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 4-67 1.49e-29

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 114.47  E-value: 1.49e-29
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1503143914   4 DYYSILEVTPNASINDIKKSYRKLALKWHPDKNPENQEqANRMFKEISEAYEVLSDEAKRKLYD 67
Cdd:PRK10767    5 DYYEVLGVSRNASEDEIKKAYRKLAMKYHPDRNPGDKE-AEEKFKEIKEAYEVLSDPQKRAAYD 67
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
 4-68 1.02e-27

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: 109.23  E-value: 1.02e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1503143914   4 DYYSILEVTPNASINDIKKSYRKLALKWHPDKNPEnqEQANRMFKEISEAYEVLSDEAKRKLYDE 68
Cdd:TIGR02349   1 DYYEILGVSKDASEEEIKKAYRKLAKKYHPDRNKD--KEAEEKFKEINEAYEVLSDPEKRAQYDQ 63
DnaJ smart00271
DnaJ molecular chaperone homology domain;
4-62 4.11e-27

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 99.62  E-value: 4.11e-27
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1503143914    4 DYYSILEVTPNASINDIKKSYRKLALKWHPDKNPENQEQANRMFKEISEAYEVLSDEAK 62
Cdd:smart00271   2 DYYEILGVPRDASLDEIKKAYRKLALKYHPDKNPGDKEEAEEKFKEINEAYEVLSDPEK 60
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
4-80 5.08e-26

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


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 97.87  E-value: 5.08e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1503143914   4 DYYSILEVTPNASINDIKKSYRKLALKWHPDKNPENQEQANRMFKEISEAYEVLSDEAKRKLYD----EQRKRKVSASSR 79
Cdd:COG2214     6 DHYAVLGVPPDASLEEIRQAYRRLAKLLHPDRGGELKALAEELFQRLNEAYEVLSDPERRAEYDrelgQSGKGSASQPSA 85


                  .
gi 1503143914  80 P 80
Cdd:COG2214    86 A 86
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 4-59 1.32e-24

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: 92.99  E-value: 1.32e-24
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1503143914   4 DYYSILEVTPNASINDIKKSYRKLALKWHPDKNPENqEQANRMFKEISEAYEVLSD 59
Cdd:cd06257     1 DYYDILGVPPDASDEEIKKAYRKLALKYHPDKNPDD-PEAEEKFKEINEAYEVLSD 55
PRK14290 PRK14290
chaperone protein DnaJ; Provisional
 1-104 2.34e-24

chaperone protein DnaJ; Provisional


Pssm-ID: 172778 [Multi-domain]  Cd Length: 365  Bit Score: 100.39  E-value: 2.34e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1503143914   1 MSGDYYSILEVTPNASINDIKKSYRKLALKWHPDKNPENQEQANRMFKEISEAYEVLSDEAKRKLYDEQRKRKVSASSRP 80
Cdd:PRK14290    1 MAKDYYKILGVDRNASQEDIKKAFRELAKKWHPDLHPGNKAEAEEKFKEISEAYEVLSDPQKRRQYDQTGTVDFGAGGSN 80

                          90       100
                  ....*....|....*....|....
gi 1503143914  81 FFYNFFEspfhrYFDKKRKAYNQY 104
Cdd:PRK14290   81 FNWDNFT-----HFSDINDIFNQI 99
PRK14281 PRK14281
chaperone protein DnaJ; Provisional
 1-68 1.73e-23

chaperone protein DnaJ; Provisional


Pssm-ID: 237657 [Multi-domain]  Cd Length: 397  Bit Score: 98.34  E-value: 1.73e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1503143914   1 MSGDYYSILEVTPNASINDIKKSYRKLALKWHPDKNPENQEqANRMFKEISEAYEVLSDEAKRKLYDE 68
Cdd:PRK14281    1 MKRDYYEVLGVSRSADKDEIKKAYRKLALKYHPDKNPDNKE-AEEHFKEVNEAYEVLSNDDKRRRYDQ 67
PRK14284 PRK14284
chaperone protein DnaJ; Provisional
 4-71 2.99e-23

chaperone protein DnaJ; Provisional


Pssm-ID: 237658 [Multi-domain]  Cd Length: 391  Bit Score: 97.61  E-value: 2.99e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1503143914   4 DYYSILEVTPNASINDIKKSYRKLALKWHPDKNPENQEqANRMFKEISEAYEVLSDEAKRKLYDEQRK 71
Cdd:PRK14284    2 DYYTILGVSKTASPEEIKKAYRKLAVKYHPDKNPGDAE-AEKRFKEVSEAYEVLSDAQKRESYDRYGK 68
PRK14282 PRK14282
chaperone protein DnaJ; Provisional
 4-92 3.71e-23

chaperone protein DnaJ; Provisional


Pssm-ID: 184603 [Multi-domain]  Cd Length: 369  Bit Score: 97.17  E-value: 3.71e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1503143914   4 DYYSILEVTPNASINDIKKSYRKLALKWHPDKNPENQEQANRMFKEISEAYEVLSDEAKRKLYD------EQRKRKVSAS 77
Cdd:PRK14282    5 DYYEILGVSRNATQEEIKRAYKRLVKEWHPDRHPENRKEAEQKFKEIQEAYEVLSDPQKRAMYDrfgyvgEQPPYQETES 84

                          90
                  ....*....|....*...
gi 1503143914  78 SRPFF---YNFFESPFHR 92
Cdd:PRK14282   85 GGGFFediFKDFENIFNR 102
PRK14291 PRK14291
chaperone protein DnaJ; Provisional
 4-68 5.17e-23

chaperone protein DnaJ; Provisional


Pssm-ID: 237661 [Multi-domain]  Cd Length: 382  Bit Score: 96.76  E-value: 5.17e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1503143914   4 DYYSILEVTPNASINDIKKSYRKLALKWHPD--KNPENQEQanrmFKEISEAYEVLSDEAKRKLYDE 68
Cdd:PRK14291    4 DYYEILGVSRNATQEEIKKAYRRLARKYHPDfnKNPEAEEK----FKEINEAYQVLSDPEKRKLYDQ 66
PRK14294 PRK14294
chaperone protein DnaJ; Provisional
 4-68 7.67e-23

chaperone protein DnaJ; Provisional


Pssm-ID: 237664 [Multi-domain]  Cd Length: 366  Bit Score: 95.99  E-value: 7.67e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1503143914   4 DYYSILEVTPNASINDIKKSYRKLALKWHPDKNPENQEqANRMFKEISEAYEVLSDEAKRKLYDE 68
Cdd:PRK14294    5 DYYEILGVTRDASEEEIKKSYRKLAMKYHPDRNPGDKE-AEELFKEAAEAYEVLSDPKKRGIYDQ 68
PRK14279 PRK14279
molecular chaperone DnaJ;
4-71 1.00e-22

molecular chaperone DnaJ;


Pssm-ID: 237655 [Multi-domain]  Cd Length: 392  Bit Score: 95.95  E-value: 1.00e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1503143914   4 DYYSILEVTPNASINDIKKSYRKLALKWHPDKNPENQEQANRmFKEISEAYEVLSDEAKRKLYDEQRK 71
Cdd:PRK14279   10 DFYKELGVSSDASAEEIKKAYRKLARELHPDANPGDPAAEER-FKAVSEAHDVLSDPAKRKEYDETRR 76
PRK14295 PRK14295
molecular chaperone DnaJ;
4-80 1.03e-22

molecular chaperone DnaJ;


Pssm-ID: 237665 [Multi-domain]  Cd Length: 389  Bit Score: 96.07  E-value: 1.03e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1503143914   4 DYYSILEVTPNASINDIKKSYRKLALKWHPDKNPENQEQANRmFKEISEAYEVLSDEAKRKLYDEQRKRKVSASSRP 80
Cdd:PRK14295   10 DYYKVLGVPKDATEAEIKKAYRKLAREYHPDANKGDAKAEER-FKEISEAYDVLSDEKKRKEYDEARSLFGNGGFRP 85
SEC63 COG5407
Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular ...
 4-64 1.35e-22

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


Pssm-ID: 444165 [Multi-domain]  Cd Length: 61  Bit Score: 88.13  E-value: 1.35e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1503143914   4 DYYSILEVTPNASINDIKKSYRKLALKWHPDKNPENQeQANRMFKEISEAYEVLSDEAKRK 64
Cdd:COG5407     1 DPYEVLGVAKTASADEIKKAYRKLAKKYHPDRNKGDP-KAEERFKEINEAYELLSDAEKRA 60
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
 4-67 2.82e-22

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 94.53  E-value: 2.82e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1503143914   4 DYYSILEVTPNASINDIKKSYRKLALKWHPDKNPEnqEQANRMFKEISEAYEVLSDEAKRKLYD 67
Cdd:PRK14298    6 DYYEILGLSKDASVEDIKKAYRKLAMKYHPDKNKE--PDAEEKFKEISEAYAVLSDAEKRAQYD 67
PRK14278 PRK14278
chaperone protein DnaJ; Provisional
 1-67 2.93e-22

chaperone protein DnaJ; Provisional


Pssm-ID: 237654 [Multi-domain]  Cd Length: 378  Bit Score: 94.73  E-value: 2.93e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1503143914   1 MSGDYYSILEVTPNASINDIKKSYRKLALKWHPDKNPENQEQANrmFKEISEAYEVLSDEAKRKLYD 67
Cdd:PRK14278    1 MARDYYGLLGVSRNASDAEIKRAYRKLARELHPDVNPDEEAQEK--FKEISVAYEVLSDPEKRRIVD 65
PRK14277 PRK14277
chaperone protein DnaJ; Provisional
 4-68 1.91e-21

chaperone protein DnaJ; Provisional


Pssm-ID: 184599 [Multi-domain]  Cd Length: 386  Bit Score: 92.56  E-value: 1.91e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1503143914   4 DYYSILEVTPNASINDIKKSYRKLALKWHPDKNPENQEqANRMFKEISEAYEVLSDEAKRKLYDE 68
Cdd:PRK14277    6 DYYEILGVDRNATEEEIKKAYRRLAKKYHPDLNPGDKE-AEQKFKEINEAYEILSDPQKRAQYDQ 69
PRK14301 PRK14301
chaperone protein DnaJ; Provisional
 4-67 2.03e-21

chaperone protein DnaJ; Provisional


Pssm-ID: 237668 [Multi-domain]  Cd Length: 373  Bit Score: 92.11  E-value: 2.03e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1503143914   4 DYYSILEVTPNASINDIKKSYRKLALKWHPDKNPENQEqANRMFKEISEAYEVLSDEAKRKLYD 67
Cdd:PRK14301    5 DYYEVLGVSRDASEDEIKKAYRKLALQYHPDRNPDNPE-AEQKFKEAAEAYEVLRDAEKRARYD 67
PRK14289 PRK14289
molecular chaperone DnaJ;
4-68 3.12e-21

molecular chaperone DnaJ;


Pssm-ID: 237660 [Multi-domain]  Cd Length: 386  Bit Score: 91.82  E-value: 3.12e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1503143914   4 DYYSILEVTPNASINDIKKSYRKLALKWHPDKNPENQEqANRMFKEISEAYEVLSDEAKRKLYDE 68
Cdd:PRK14289    6 DYYEVLGVSKTATVDEIKKAYRKKAIQYHPDKNPGDKE-AEEKFKEAAEAYDVLSDPDKRSRYDQ 69
PRK14280 PRK14280
molecular chaperone DnaJ;
4-68 5.92e-21

molecular chaperone DnaJ;


Pssm-ID: 237656 [Multi-domain]  Cd Length: 376  Bit Score: 90.94  E-value: 5.92e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1503143914   4 DYYSILEVTPNASINDIKKSYRKLALKWHPDKNPEnqEQANRMFKEISEAYEVLSDEAKRKLYDE 68
Cdd:PRK14280    5 DYYEVLGVSKSASKDEIKKAYRKLSKKYHPDINKE--EGADEKFKEISEAYEVLSDDQKRAQYDQ 67
PRK14283 PRK14283
chaperone protein DnaJ; Provisional
 4-68 3.47e-20

chaperone protein DnaJ; Provisional


Pssm-ID: 184604 [Multi-domain]  Cd Length: 378  Bit Score: 88.73  E-value: 3.47e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1503143914   4 DYYSILEVTPNASINDIKKSYRKLALKWHPDKNPEnqEQANRMFKEISEAYEVLSDEAKRKLYDE 68
Cdd:PRK14283    6 DYYEVLGVDRNADKKEIKKAYRKLARKYHPDVSEE--EGAEEKFKEISEAYAVLSDDEKRQRYDQ 68
PRK10266 PRK10266
curved DNA-binding protein;
4-107 9.71e-20

curved DNA-binding protein;


Pssm-ID: 182347 [Multi-domain]  Cd Length: 306  Bit Score: 86.80  E-value: 9.71e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1503143914   4 DYYSILEVTPNASINDIKKSYRKLALKWHPDKNPENQEQANrmFKEISEAYEVLSDEAKRKLYDEQRKRK---------- 73
Cdd:PRK10266    5 DYYAIMGVKPTDDLKTIKTAYRRLARKYHPDVSKEPDAEAR--FKEVAEAWEVLSDEQRRAEYDQLWQHRndpqfnrqfq 82

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1503143914  74 ---VSASSRPFFYNFFESPFHRYFDKKRKAYNQYGKD 107
Cdd:PRK10266   83 hgdGQSFNAEDFDDIFSSIFGQHARQSRQRPAARGHD 119
PRK14297 PRK14297
molecular chaperone DnaJ;
2-68 2.68e-19

molecular chaperone DnaJ;


Pssm-ID: 184611 [Multi-domain]  Cd Length: 380  Bit Score: 86.38  E-value: 2.68e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1503143914   2 SGDYYSILEVTPNASINDIKKSYRKLALKWHPDKNPENQEqANRMFKEISEAYEVLSDEAKRKLYDE 68
Cdd:PRK14297    3 SKDYYEVLGLEKGASDDEIKKAFRKLAIKYHPDKNKGNKE-AEEKFKEINEAYQVLSDPQKKAQYDQ 68
PRK14293 PRK14293
molecular chaperone DnaJ;
1-67 6.34e-19

molecular chaperone DnaJ;


Pssm-ID: 237663 [Multi-domain]  Cd Length: 374  Bit Score: 85.04  E-value: 6.34e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1503143914   1 MSGDYYSILEVTPNASINDIKKSYRKLALKWHPDKNPEnqEQANRMFKEISEAYEVLSDEAKRKLYD 67
Cdd:PRK14293    1 MAADYYEILGVSRDADKDELKRAYRRLARKYHPDVNKE--PGAEDRFKEINRAYEVLSDPETRARYD 65
PTZ00037 PTZ00037
DnaJ_C chaperone protein; Provisional
 5-68 9.89e-19

DnaJ_C chaperone protein; Provisional


Pssm-ID: 240236 [Multi-domain]  Cd Length: 421  Bit Score: 84.87  E-value: 9.89e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1503143914   5 YYSILEVTPNASINDIKKSYRKLALKWHPDK--NPEnqeqanrMFKEISEAYEVLSDEAKRKLYDE 68
Cdd:PTZ00037   30 LYEVLNLSKDCTTSEIKKAYRKLAIKHHPDKggDPE-------KFKEISRAYEVLSDPEKRKIYDE 88
terminal_TopJ NF037946
terminal organelle assembly protein TopJ;
4-67 1.02e-18

terminal organelle assembly protein TopJ;


Pssm-ID: 468284 [Multi-domain]  Cd Length: 440  Bit Score: 85.26  E-value: 1.02e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1503143914   4 DYYSILEVTPNASINDIKKSYRKLALKWHPDKNpeNQEQANRMFKEISEAYEVLSDEAKRKLYD 67
Cdd:NF037946    6 DYYEVLGVDRDADDQEIKKAFRKLAKKYHPDRN--KAPDAAEIFAEINEAYEVLSNPEKRANYD 67
PRK14299 PRK14299
chaperone protein DnaJ; Provisional
 4-67 1.13e-18

chaperone protein DnaJ; Provisional


Pssm-ID: 237667 [Multi-domain]  Cd Length: 291  Bit Score: 83.45  E-value: 1.13e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1503143914   4 DYYSILEVTPNASINDIKKSYRKLALKWHPD--KNPENQEQanrmFKEISEAYEVLSDEAKRKLYD 67
Cdd:PRK14299    5 DYYAILGVPKNASQDEIKKAFKKLARKYHPDvnKSPGAEEK----FKEINEAYTVLSDPEKRRIYD 66
PRK14276 PRK14276
chaperone protein DnaJ; Provisional
 4-68 1.15e-18

chaperone protein DnaJ; Provisional


Pssm-ID: 237653 [Multi-domain]  Cd Length: 380  Bit Score: 84.37  E-value: 1.15e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1503143914   4 DYYSILEVTPNASINDIKKSYRKLALKWHPDKNPEnqEQANRMFKEISEAYEVLSDEAKRKLYDE 68
Cdd:PRK14276    5 EYYDRLGVSKDASQDEIKKAYRKLSKKYHPDINKE--PGAEEKYKEVQEAYETLSDPQKRAAYDQ 67
PRK14286 PRK14286
chaperone protein DnaJ; Provisional
 5-81 2.15e-18

chaperone protein DnaJ; Provisional


Pssm-ID: 172774 [Multi-domain]  Cd Length: 372  Bit Score: 83.89  E-value: 2.15e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1503143914   5 YYSILEVTPNASINDIKKSYRKLALKWHPDKNPENQEqANRMFKEISEAYEVLSDEAKRKLYDEQRKRKVSASSRPF 81
Cdd:PRK14286    6 YYDILGVSKSANDEEIKSAYRKLAIKYHPDKNKGNKE-SEEKFKEATEAYEILRDPKKRQAYDQFGKAGVNAGAGGF 81
PRK14292 PRK14292
chaperone protein DnaJ; Provisional
 4-67 8.10e-18

chaperone protein DnaJ; Provisional


Pssm-ID: 237662 [Multi-domain]  Cd Length: 371  Bit Score: 82.24  E-value: 8.10e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1503143914   4 DYYSILEVTPNASINDIKKSYRKLALKWHPDKNPEnqEQANRMFKEISEAYEVLSDEAKRKLYD 67
Cdd:PRK14292    3 DYYELLGVSRTASADEIKSAYRKLALKYHPDRNKE--KGAAEKFAQINEAYAVLSDAEKRAHYD 64
PRK14285 PRK14285
chaperone protein DnaJ; Provisional
 1-67 1.57e-17

chaperone protein DnaJ; Provisional


Pssm-ID: 172773 [Multi-domain]  Cd Length: 365  Bit Score: 81.19  E-value: 1.57e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1503143914   1 MSGDYYSILEVTPNASINDIKKSYRKLALKWHPDKNPENQEqANRMFKEISEAYEVLSDEAKRKLYD 67
Cdd:PRK14285    1 MKRDYYEILGLSKGASKDEIKKAYRKIAIKYHPDKNKGNKE-AESIFKEATEAYEVLIDDNKRAQYD 66
PRK14288 PRK14288
molecular chaperone DnaJ;
1-87 4.18e-16

molecular chaperone DnaJ;


Pssm-ID: 172776 [Multi-domain]  Cd Length: 369  Bit Score: 77.04  E-value: 4.18e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1503143914   1 MSGDYYSILEVTPNASINDIKKSYRKLALKWHPDKNPENQEQANRmFKEISEAYEVLSDEAKRKLYDEQRKRKV--SASS 78
Cdd:PRK14288    1 MELSYYEILEVEKHSNQETIKKSYRKLALKYHPDRNAGDKEAEEK-FKLINEAYGVLSDEKKRALYDRYGKKGLnqAGAS 79


                  ....*....
gi 1503143914  79 RPFFYNFFE 87
Cdd:PRK14288   80 QSDFSDFFE 88
termin_org_DnaJ TIGR03835
terminal organelle assembly protein TopJ; This model describes TopJ (MG_200, CbpA), a DnaJ ...
 4-68 7.66e-16

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: 77.16  E-value: 7.66e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1503143914   4 DYYSILEVTPNASINDIKKSYRKLALKWHPDKNpeNQEQANRMFKEISEAYEVLSDEAKRKLYDE 68
Cdd:TIGR03835   3 DYYEVLGIDRDADEQEIKKAFRKLAKKYHPDRN--KAPDAASIFAEINEANDVLSNPKKRANYDK 65
PRK14287 PRK14287
chaperone protein DnaJ; Provisional
 4-68 1.64e-14

chaperone protein DnaJ; Provisional


Pssm-ID: 237659 [Multi-domain]  Cd Length: 371  Bit Score: 72.73  E-value: 1.64e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1503143914   4 DYYSILEVTPNASINDIKKSYRKLALKWHPDKNPEnqEQANRMFKEISEAYEVLSDEAKRKLYDE 68
Cdd:PRK14287    5 DYYEVLGVDRNASVDEVKKAYRKLARKYHPDVNKA--PDAEDKFKEVKEAYDTLSDPQKKAHYDQ 67
PRK14300 PRK14300
chaperone protein DnaJ; Provisional
 1-67 2.39e-14

chaperone protein DnaJ; Provisional


Pssm-ID: 172788 [Multi-domain]  Cd Length: 372  Bit Score: 71.97  E-value: 2.39e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1503143914   1 MSGDYYSILEVTPNASINDIKKSYRKLALKWHPDKNpeNQEQANRMFKEISEAYEVLSDEAKRKLYD 67
Cdd:PRK14300    1 MSQDYYQILGVSKTASQADLKKAYLKLAKQYHPDTT--DAKDAEKKFKEINAAYDVLKDEQKRAAYD 65
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
4-65 1.22e-13

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


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 64.43  E-value: 1.22e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1503143914   4 DYYSILEVTPNASINDIKKSYRKLALKWHPDK-----NPENQEQANRMFKEISEAYEVLSDEAKRKL 65
Cdd:COG1076     5 DAFELLGLPPDADDAELKRAYRKLQREHHPDRlaaglPEEEQRLALQKAAAINEAYETLKDPRGIDL 71
PRK14296 PRK14296
chaperone protein DnaJ; Provisional
 4-68 3.16e-11

chaperone protein DnaJ; Provisional


Pssm-ID: 237666 [Multi-domain]  Cd Length: 372  Bit Score: 63.04  E-value: 3.16e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1503143914   4 DYYSILEVTPNASINDIKKSYRKLALKWHPDKNPENqeQANRMFKEISEAYEVLSDEAKRKLYDE 68
Cdd:PRK14296    5 DYYEVLGVSKTASEQEIRQAYRKLAKQYHPDLNKSP--DAHDKMVEINEAADVLLDKDKRKQYDQ 67
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
 5-68 3.67e-09

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 57.10  E-value: 3.67e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1503143914    5 YYSILEVTPNASINDIKKSYRKLALKWHPDKNPENQEQANrmFKEISEAYEVLSDEAKRKLYDE 68
Cdd:PTZ00341   575 FYDILGVGVNADMKEISERYFKLAENYYPPKRSGNEGFHK--FKKINEAYQILGDIDKKKMYNK 636
djlA PRK09430
co-chaperone DjlA;
4-57 4.33e-08

co-chaperone DjlA;


Pssm-ID: 236512 [Multi-domain]  Cd Length: 267  Bit Score: 52.89  E-value: 4.33e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1503143914   4 DYYSILEVTPNASINDIKKSYRKLALKWHPDK------NPENQEQANRMFKEISEAYEVL 57
Cdd:PRK09430  201 DAYKVLGVSESDDDQEIKRAYRKLMSEHHPDKlvakglPPEMMEMAKEKAQEIQAAYELI 260
ZUO1 COG5269
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ...
 4-67 3.28e-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: 41.56  E-value: 3.28e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1503143914   4 DYYSILEVTP---NASINDIKKSYRKLALKWHPDKNPENQEQANR-MFKEISEAYEVLSDEAKRKLYD 67
Cdd:COG5269    44 DLYALLGLSKyrtKAIPPQILKAHKKKVYKYHPDKTAAGGNKGCDeFFKLIQKAREVLGDRKLRLQYD 111
hscB PRK01356
co-chaperone HscB; Provisional
 4-87 1.06e-03

co-chaperone HscB; Provisional


Pssm-ID: 167217 [Multi-domain]  Cd Length: 166  Bit Score: 38.70  E-value: 1.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1503143914   4 DYYSILEVTPNASIN--DIKKSYRKLALKWHPD--KNPENQEQANRMFKEISEAYEVLSDEAKRKLY----------DEQ 69
Cdd:PRK01356    3 NYFQLLGLPQEYNIDlkILEKQYFAMQVKYHPDkaKTLQEKEQNLIIASELNNAYSTLKDALKRAEYmlllqninlnDEK 82

                          90
                  ....*....|....*...
gi 1503143914  70 RKRKVSASSRPFFYNFFE 87
Cdd:PRK01356   83 TRSLLSPLELSIFWDEME 100
PHA03102 PHA03102
Small T antigen; Reviewed
 7-60 1.34e-03

Small T antigen; Reviewed


Pssm-ID: 222986 [Multi-domain]  Cd Length: 153  Bit Score: 38.50  E-value: 1.34e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1503143914   7 SILEVTPNASIN--DIKKSYRKLALKWHPDK--NPENQEQANRMFKEISEAYEVLSDE 60
Cdd:PHA03102    9 DLLGLPRSAWGNlpLMRKAYLRKCLEFHPDKggDEEKMKELNTLYKKFRESVKSLRDL 66
hscB TIGR00714
Fe-S protein assembly co-chaperone HscB; This model describes the small subunit, Hsc20 (20K ...
 20-66 3.65e-03

Fe-S protein assembly co-chaperone HscB; This model describes the small subunit, Hsc20 (20K heat shock cognate protein) of a pair of proteins Hsc66-Hsc20, related to the DnaK-DnaJ heat shock proteins, which also serve as molecular chaperones. Hsc20, unlike DnaJ, appears not to have chaperone activity on its own, but to act solely as a regulatory subunit for Hsc66 (i.e., to be a co-chaperone). The gene for Hsc20 in E. coli, hscB, is not induced by heat shock. [Protein fate, Protein folding and stabilization]


Pssm-ID: 211601 [Multi-domain]  Cd Length: 155  Bit Score: 37.17  E-value: 3.65e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1503143914  20 IKKSYRKLALKWHPDKNPENQEQANRMFK--EISEAYEVLSDEAKRKLY 66
Cdd:TIGR00714   8 LRKRYRQLQAQYHPDASGMAQEQLAASQQstTLNQAYHTLKDPLRRAEY 56
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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