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Conserved domains on  [gi|112293277|ref|NP_055095|]
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dnaJ homolog subfamily C member 8 [Homo sapiens]

Protein Classification

J domain-containing protein( domain architecture ID 11454581)

J domain-containing protein similar to molecular chaperone DnaJ; DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and play crucial roles in protein translation, folding, unfolding, translocation, and degradation

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 57-112 8.80e-15

DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and play crucial roles in protein translation, folding, unfolding, translocation, and degradation. They act primarily by stimulating the ATPase activity of Hsp70s, an important chaperonine family. Hsp40 proteins are characterized by the presence of a J domain, which mediates the interaction with Hsp70. They may contain other domains as well, and the architectures provide a means of classification.


:

Pssm-ID: 99751 [Multi-domain]  Cd Length: 55  Bit Score: 66.80  E-value: 8.80e-15
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 112293277  57 NPFEVLQIDPEVTDEEIKKRFRQLSILVHPDKNQDDADrAQKAFEAVDKAYKLLLD 112
Cdd:cd06257    1 DYYDILGVPPDASDEEIKKAYRKLALKYHPDKNPDDPE-AEEKFKEINEAYEVLSD 55
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 57-184 1.31e-10

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: 57.79  E-value: 1.31e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293277  57 NPFEVLQIDPEVTDEEIKKRFRQLSILVHPDKNQDDADRAQKaFEAVDKAYKLLLDQEQKKRALDVIQAGKEYVEHTVKE 136
Cdd:COG0484    1 DYYEILGVSRDASAEEIKKAYRKLAKKYHPDRNPGDPEAEEK-FKEINEAYEVLSDPEKRAAYDRFGHAAELLLATELAE 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 112293277 137 RKKQLKKEGKPTIVEEDDPELFKQAVYKQTMKLFAELEIKRKEREAKE 184
Cdd:COG0484   80 SAAAEAAAAEAKEEAAEAGASEYEAIAEEASQLRLASLLLLLALLELA 127
 
Name Accession Description Interval E-value
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 57-112 8.80e-15

DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and play crucial roles in protein translation, folding, unfolding, translocation, and degradation. They act primarily by stimulating the ATPase activity of Hsp70s, an important chaperonine family. Hsp40 proteins are characterized by the presence of a J domain, which mediates the interaction with Hsp70. They may contain other domains as well, and the architectures provide a means of classification.


Pssm-ID: 99751 [Multi-domain]  Cd Length: 55  Bit Score: 66.80  E-value: 8.80e-15
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 112293277  57 NPFEVLQIDPEVTDEEIKKRFRQLSILVHPDKNQDDADrAQKAFEAVDKAYKLLLD 112
Cdd:cd06257    1 DYYDILGVPPDASDEEIKKAYRKLALKYHPDKNPDDPE-AEEKFKEINEAYEVLSD 55
DnaJ smart00271
DnaJ molecular chaperone homology domain;
57-115 1.45e-13

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 63.41  E-value: 1.45e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 112293277    57 NPFEVLQIDPEVTDEEIKKRFRQLSILVHPDKNQDDADRAQKAFEAVDKAYKLLLDQEQ 115
Cdd:smart00271   2 DYYEILGVPRDASLDEIKKAYRKLALKYHPDKNPGDKEEAEEKFKEINEAYEVLSDPEK 60
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 57-121 1.64e-13

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: 63.65  E-value: 1.64e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 112293277   57 NPFEVLQIDPEVTDEEIKKRFRQLSILVHPDKNQDDADrAQKAFEAVDKAYKLLLDqEQKKRALD 121
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNPGDPE-AEEKFKEINEAYEVLSD-PEKRAIYD 63
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 57-184 1.31e-10

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: 57.79  E-value: 1.31e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293277  57 NPFEVLQIDPEVTDEEIKKRFRQLSILVHPDKNQDDADRAQKaFEAVDKAYKLLLDQEQKKRALDVIQAGKEYVEHTVKE 136
Cdd:COG0484    1 DYYEILGVSRDASAEEIKKAYRKLAKKYHPDRNPGDPEAEEK-FKEINEAYEVLSDPEKRAAYDRFGHAAELLLATELAE 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 112293277 137 RKKQLKKEGKPTIVEEDDPELFKQAVYKQTMKLFAELEIKRKEREAKE 184
Cdd:COG0484   80 SAAAEAAAAEAKEEAAEAGASEYEAIAEEASQLRLASLLLLLALLELA 127
SEC63 COG5407
Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular ...
 57-118 1.55e-10

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


Pssm-ID: 444165 [Multi-domain]  Cd Length: 61  Bit Score: 55.39  E-value: 1.55e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 112293277  57 NPFEVLQIDPEVTDEEIKKRFRQLSILVHPDKNQDDADrAQKAFEAVDKAYKLLLDQEQKKR 118
Cdd:COG5407    1 DPYEVLGVAKTASADEIKKAYRKLAKKYHPDRNKGDPK-AEERFKEINEAYELLSDAEKRAR 61
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 59-132 4.31e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 59.00  E-value: 4.31e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 112293277  59 FEVLQIDPEVTDEEIKKRFRQLSILVHPDKNQDDADrAQKAFEAVDKAYKLLLDqEQKKRALDviQAGKEYVEH 132
Cdd:PRK10767   7 YEVLGVSRNASEDEIKKAYRKLAMKYHPDRNPGDKE-AEEKFKEIKEAYEVLSD-PQKRAAYD--QYGHAAFEQ 76
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
 59-128 2.15e-07

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: 51.06  E-value: 2.15e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293277   59 FEVLQIDPEVTDEEIKKRFRQLSILVHPDKNQDDAdrAQKAFEAVDKAYKLLLDqEQKKRALDviQAGKE 128
Cdd:TIGR02349   3 YEILGVSKDASEEEIKKAYRKLAKKYHPDRNKDKE--AEEKFKEINEAYEVLSD-PEKRAQYD--QFGHA 67
 
Name Accession Description Interval E-value
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 57-112 8.80e-15

DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and play crucial roles in protein translation, folding, unfolding, translocation, and degradation. They act primarily by stimulating the ATPase activity of Hsp70s, an important chaperonine family. Hsp40 proteins are characterized by the presence of a J domain, which mediates the interaction with Hsp70. They may contain other domains as well, and the architectures provide a means of classification.


Pssm-ID: 99751 [Multi-domain]  Cd Length: 55  Bit Score: 66.80  E-value: 8.80e-15
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 112293277  57 NPFEVLQIDPEVTDEEIKKRFRQLSILVHPDKNQDDADrAQKAFEAVDKAYKLLLD 112
Cdd:cd06257    1 DYYDILGVPPDASDEEIKKAYRKLALKYHPDKNPDDPE-AEEKFKEINEAYEVLSD 55
DnaJ smart00271
DnaJ molecular chaperone homology domain;
57-115 1.45e-13

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 63.41  E-value: 1.45e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 112293277    57 NPFEVLQIDPEVTDEEIKKRFRQLSILVHPDKNQDDADRAQKAFEAVDKAYKLLLDQEQ 115
Cdd:smart00271   2 DYYEILGVPRDASLDEIKKAYRKLALKYHPDKNPGDKEEAEEKFKEINEAYEVLSDPEK 60
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 57-121 1.64e-13

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: 63.65  E-value: 1.64e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 112293277   57 NPFEVLQIDPEVTDEEIKKRFRQLSILVHPDKNQDDADrAQKAFEAVDKAYKLLLDqEQKKRALD 121
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNPGDPE-AEEKFKEINEAYEVLSD-PEKRAIYD 63
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 57-184 1.31e-10

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: 57.79  E-value: 1.31e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293277  57 NPFEVLQIDPEVTDEEIKKRFRQLSILVHPDKNQDDADRAQKaFEAVDKAYKLLLDQEQKKRALDVIQAGKEYVEHTVKE 136
Cdd:COG0484    1 DYYEILGVSRDASAEEIKKAYRKLAKKYHPDRNPGDPEAEEK-FKEINEAYEVLSDPEKRAAYDRFGHAAELLLATELAE 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 112293277 137 RKKQLKKEGKPTIVEEDDPELFKQAVYKQTMKLFAELEIKRKEREAKE 184
Cdd:COG0484   80 SAAAEAAAAEAKEEAAEAGASEYEAIAEEASQLRLASLLLLLALLELA 127
SEC63 COG5407
Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular ...
 57-118 1.55e-10

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


Pssm-ID: 444165 [Multi-domain]  Cd Length: 61  Bit Score: 55.39  E-value: 1.55e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 112293277  57 NPFEVLQIDPEVTDEEIKKRFRQLSILVHPDKNQDDADrAQKAFEAVDKAYKLLLDQEQKKR 118
Cdd:COG5407    1 DPYEVLGVAKTASADEIKKAYRKLAKKYHPDRNKGDPK-AEERFKEINEAYELLSDAEKRAR 61
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
57-118 2.30e-10

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


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 55.88  E-value: 2.30e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 112293277  57 NPFEVLQIDPEVTDEEIKKRFRQLSILVHPDKNQDDADRAQKAFEAVDKAYKLLLDQEQKKR 118
Cdd:COG2214    6 DHYAVLGVPPDASLEEIRQAYRRLAKLLHPDRGGELKALAEELFQRLNEAYEVLSDPERRAE 67
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 59-132 4.31e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 59.00  E-value: 4.31e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 112293277  59 FEVLQIDPEVTDEEIKKRFRQLSILVHPDKNQDDADrAQKAFEAVDKAYKLLLDqEQKKRALDviQAGKEYVEH 132
Cdd:PRK10767   7 YEVLGVSRNASEDEIKKAYRKLAMKYHPDRNPGDKE-AEEKFKEIKEAYEVLSD-PQKRAAYD--QYGHAAFEQ 76
PRK14297 PRK14297
molecular chaperone DnaJ;
59-118 1.28e-09

molecular chaperone DnaJ;


Pssm-ID: 184611 [Multi-domain]  Cd Length: 380  Bit Score: 57.87  E-value: 1.28e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293277  59 FEVLQIDPEVTDEEIKKRFRQLSILVHPDKNQDDADrAQKAFEAVDKAYKLLLDQEQKKR 118
Cdd:PRK14297   7 YEVLGLEKGASDDEIKKAFRKLAIKYHPDKNKGNKE-AEEKFKEINEAYQVLSDPQKKAQ 65
PRK14284 PRK14284
chaperone protein DnaJ; Provisional
 59-121 4.05e-09

chaperone protein DnaJ; Provisional


Pssm-ID: 237658 [Multi-domain]  Cd Length: 391  Bit Score: 56.39  E-value: 4.05e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 112293277  59 FEVLQIDPEVTDEEIKKRFRQLSILVHPDKNQDDADrAQKAFEAVDKAYKLLLDqEQKKRALD 121
Cdd:PRK14284   4 YTILGVSKTASPEEIKKAYRKLAVKYHPDKNPGDAE-AEKRFKEVSEAYEVLSD-AQKRESYD 64
PRK14289 PRK14289
molecular chaperone DnaJ;
59-118 7.12e-09

molecular chaperone DnaJ;


Pssm-ID: 237660 [Multi-domain]  Cd Length: 386  Bit Score: 55.61  E-value: 7.12e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293277  59 FEVLQIDPEVTDEEIKKRFRQLSILVHPDKNQDDADrAQKAFEAVDKAYKLLLDQEQKKR 118
Cdd:PRK14289   8 YEVLGVSKTATVDEIKKAYRKKAIQYHPDKNPGDKE-AEEKFKEAAEAYDVLSDPDKRSR 66
PRK14281 PRK14281
chaperone protein DnaJ; Provisional
 59-118 8.39e-09

chaperone protein DnaJ; Provisional


Pssm-ID: 237657 [Multi-domain]  Cd Length: 397  Bit Score: 55.20  E-value: 8.39e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293277  59 FEVLQIDPEVTDEEIKKRFRQLSILVHPDKNQDDADrAQKAFEAVDKAYKLLLDQEQKKR 118
Cdd:PRK14281   6 YEVLGVSRSADKDEIKKAYRKLALKYHPDKNPDNKE-AEEHFKEVNEAYEVLSNDDKRRR 64
PRK14286 PRK14286
chaperone protein DnaJ; Provisional
 59-127 1.33e-08

chaperone protein DnaJ; Provisional


Pssm-ID: 172774 [Multi-domain]  Cd Length: 372  Bit Score: 54.61  E-value: 1.33e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 112293277  59 FEVLQIDPEVTDEEIKKRFRQLSILVHPDKNQDDADrAQKAFEAVDKAYKLLLDqEQKKRALDviQAGK 127
Cdd:PRK14286   7 YDILGVSKSANDEEIKSAYRKLAIKYHPDKNKGNKE-SEEKFKEATEAYEILRD-PKKRQAYD--QFGK 71
PRK14301 PRK14301
chaperone protein DnaJ; Provisional
 59-118 2.37e-08

chaperone protein DnaJ; Provisional


Pssm-ID: 237668 [Multi-domain]  Cd Length: 373  Bit Score: 53.98  E-value: 2.37e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293277  59 FEVLQIDPEVTDEEIKKRFRQLSILVHPDKNQDDADRAQKAFEAVDkAYKLLLDQEQKKR 118
Cdd:PRK14301   7 YEVLGVSRDASEDEIKKAYRKLALQYHPDRNPDNPEAEQKFKEAAE-AYEVLRDAEKRAR 65
PRK14278 PRK14278
chaperone protein DnaJ; Provisional
 61-121 6.39e-08

chaperone protein DnaJ; Provisional


Pssm-ID: 237654 [Multi-domain]  Cd Length: 378  Bit Score: 52.75  E-value: 6.39e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 112293277  61 VLQIDPEVTDEEIKKRFRQLSILVHPDKNQDDAdrAQKAFEAVDKAYKLLLDQEqKKRALD 121
Cdd:PRK14278   8 LLGVSRNASDAEIKRAYRKLARELHPDVNPDEE--AQEKFKEISVAYEVLSDPE-KRRIVD 65
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
 59-119 6.51e-08

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 52.54  E-value: 6.51e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 112293277  59 FEVLQIDPEVTDEEIKKRFRQLSILVHPDKNqDDADrAQKAFEAVDKAYKLLLDQEqkKRA 119
Cdd:PRK14298   8 YEILGLSKDASVEDIKKAYRKLAMKYHPDKN-KEPD-AEEKFKEISEAYAVLSDAE--KRA 64
PRK14277 PRK14277
chaperone protein DnaJ; Provisional
 59-118 7.50e-08

chaperone protein DnaJ; Provisional


Pssm-ID: 184599 [Multi-domain]  Cd Length: 386  Bit Score: 52.50  E-value: 7.50e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293277  59 FEVLQIDPEVTDEEIKKRFRQLSILVHPDKNQDDADRAQKaFEAVDKAYKLLLDQEQKKR 118
Cdd:PRK14277   8 YEILGVDRNATEEEIKKAYRRLAKKYHPDLNPGDKEAEQK-FKEINEAYEILSDPQKRAQ 66
PRK14290 PRK14290
chaperone protein DnaJ; Provisional
 59-117 1.85e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 172778 [Multi-domain]  Cd Length: 365  Bit Score: 51.09  E-value: 1.85e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 112293277  59 FEVLQIDPEVTDEEIKKRFRQLSILVHPDKNQDDADRAQKAFEAVDKAYKLLLDQEQKK 117
Cdd:PRK14290   6 YKILGVDRNASQEDIKKAFRELAKKWHPDLHPGNKAEAEEKFKEISEAYEVLSDPQKRR 64
PRK14295 PRK14295
molecular chaperone DnaJ;
53-117 1.97e-07

molecular chaperone DnaJ;


Pssm-ID: 237665 [Multi-domain]  Cd Length: 389  Bit Score: 51.00  E-value: 1.97e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 112293277  53 YFNLNPFEVLQIDPEVTDEEIKKRFRQLSILVHPDKNQDDAdRAQKAFEAVDKAYKLLLDQEQKK 117
Cdd:PRK14295   6 YIEKDYYKVLGVPKDATEAEIKKAYRKLAREYHPDANKGDA-KAEERFKEISEAYDVLSDEKKRK 69
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
 59-128 2.15e-07

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: 51.06  E-value: 2.15e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293277   59 FEVLQIDPEVTDEEIKKRFRQLSILVHPDKNQDDAdrAQKAFEAVDKAYKLLLDqEQKKRALDviQAGKE 128
Cdd:TIGR02349   3 YEILGVSKDASEEEIKKAYRKLAKKYHPDRNKDKE--AEEKFKEINEAYEVLSD-PEKRAQYD--QFGHA 67
PRK14276 PRK14276
chaperone protein DnaJ; Provisional
 59-121 1.48e-06

chaperone protein DnaJ; Provisional


Pssm-ID: 237653 [Multi-domain]  Cd Length: 380  Bit Score: 48.55  E-value: 1.48e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 112293277  59 FEVLQIDPEVTDEEIKKRFRQLSILVHPDKNQDDAdrAQKAFEAVDKAYKLLLDqEQKKRALD 121
Cdd:PRK14276   7 YDRLGVSKDASQDEIKKAYRKLSKKYHPDINKEPG--AEEKYKEVQEAYETLSD-PQKRAAYD 66
PRK14283 PRK14283
chaperone protein DnaJ; Provisional
 59-118 1.59e-06

chaperone protein DnaJ; Provisional


Pssm-ID: 184604 [Multi-domain]  Cd Length: 378  Bit Score: 48.28  E-value: 1.59e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293277  59 FEVLQIDPEVTDEEIKKRFRQLSILVHPDKNQDDAdrAQKAFEAVDKAYKLLLDQEQKKR 118
Cdd:PRK14283   8 YEVLGVDRNADKKEIKKAYRKLARKYHPDVSEEEG--AEEKFKEISEAYAVLSDDEKRQR 65
PTZ00037 PTZ00037
DnaJ_C chaperone protein; Provisional
 59-117 1.74e-06

DnaJ_C chaperone protein; Provisional


Pssm-ID: 240236 [Multi-domain]  Cd Length: 421  Bit Score: 48.28  E-value: 1.74e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 112293277  59 FEVLQIDPEVTDEEIKKRFRQLSILVHPDKNQDdadraQKAFEAVDKAYKLLLDQEQKK 117
Cdd:PTZ00037  31 YEVLNLSKDCTTSEIKKAYRKLAIKHHPDKGGD-----PEKFKEISRAYEVLSDPEKRK 84
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
57-88 3.03e-06

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


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 44.02  E-value: 3.03e-06
                         10        20        30
                 ....*....|....*....|....*....|..
gi 112293277  57 NPFEVLQIDPEVTDEEIKKRFRQLSILVHPDK 88
Cdd:COG1076    5 DAFELLGLPPDADDAELKRAYRKLQREHHPDR 36
PRK14294 PRK14294
chaperone protein DnaJ; Provisional
 59-116 4.05e-06

chaperone protein DnaJ; Provisional


Pssm-ID: 237664 [Multi-domain]  Cd Length: 366  Bit Score: 47.07  E-value: 4.05e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 112293277  59 FEVLQIDPEVTDEEIKKRFRQLSILVHPDKNQDDADrAQKAFEAVDKAYKLLLDQEQK 116
Cdd:PRK14294   7 YEILGVTRDASEEEIKKSYRKLAMKYHPDRNPGDKE-AEELFKEAAEAYEVLSDPKKR 63
PRK14280 PRK14280
molecular chaperone DnaJ;
59-121 4.48e-06

molecular chaperone DnaJ;


Pssm-ID: 237656 [Multi-domain]  Cd Length: 376  Bit Score: 47.02  E-value: 4.48e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 112293277  59 FEVLQIDPEVTDEEIKKRFRQLSILVHPDKNQdDADRAQKaFEAVDKAYKLLLDqEQKKRALD 121
Cdd:PRK14280   7 YEVLGVSKSASKDEIKKAYRKLSKKYHPDINK-EEGADEK-FKEISEAYEVLSD-DQKRAQYD 66
PRK14279 PRK14279
molecular chaperone DnaJ;
59-117 1.10e-05

molecular chaperone DnaJ;


Pssm-ID: 237655 [Multi-domain]  Cd Length: 392  Bit Score: 45.88  E-value: 1.10e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 112293277  59 FEVLQIDPEVTDEEIKKRFRQLSILVHPDKNQDDAdRAQKAFEAVDKAYKLLLDQEQKK 117
Cdd:PRK14279  12 YKELGVSSDASAEEIKKAYRKLARELHPDANPGDP-AAEERFKAVSEAHDVLSDPAKRK 69
PRK14285 PRK14285
chaperone protein DnaJ; Provisional
 59-118 1.14e-05

chaperone protein DnaJ; Provisional


Pssm-ID: 172773 [Multi-domain]  Cd Length: 365  Bit Score: 45.75  E-value: 1.14e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293277  59 FEVLQIDPEVTDEEIKKRFRQLSILVHPDKNQDDADrAQKAFEAVDKAYKLLLDQEQKKR 118
Cdd:PRK14285   6 YEILGLSKGASKDEIKKAYRKIAIKYHPDKNKGNKE-AESIFKEATEAYEVLIDDNKRAQ 64
PRK14291 PRK14291
chaperone protein DnaJ; Provisional
 59-117 1.83e-05

chaperone protein DnaJ; Provisional


Pssm-ID: 237661 [Multi-domain]  Cd Length: 382  Bit Score: 45.15  E-value: 1.83e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 112293277  59 FEVLQIDPEVTDEEIKKRFRQLSILVHPDKNQDDAdrAQKAFEAVDKAYKLLLDQEQKK 117
Cdd:PRK14291   6 YEILGVSRNATQEEIKKAYRRLARKYHPDFNKNPE--AEEKFKEINEAYQVLSDPEKRK 62
PRK14282 PRK14282
chaperone protein DnaJ; Provisional
 59-120 5.40e-05

chaperone protein DnaJ; Provisional


Pssm-ID: 184603 [Multi-domain]  Cd Length: 369  Bit Score: 43.63  E-value: 5.40e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 112293277  59 FEVLQIDPEVTDEEIKKRFRQLSILVHPDKNQDDADRAQKAFEAVDKAYKLLLDQEqkKRAL 120
Cdd:PRK14282   7 YEILGVSRNATQEEIKRAYKRLVKEWHPDRHPENRKEAEQKFKEIQEAYEVLSDPQ--KRAM 66
PRK14287 PRK14287
chaperone protein DnaJ; Provisional
 59-118 6.77e-05

chaperone protein DnaJ; Provisional


Pssm-ID: 237659 [Multi-domain]  Cd Length: 371  Bit Score: 43.46  E-value: 6.77e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293277  59 FEVLQIDPEVTDEEIKKRFRQLSILVHPDKNQddADRAQKAFEAVDKAYKLLLDQEQKKR 118
Cdd:PRK14287   7 YEVLGVDRNASVDEVKKAYRKLARKYHPDVNK--APDAEDKFKEVKEAYDTLSDPQKKAH 64
PRK14299 PRK14299
chaperone protein DnaJ; Provisional
 59-117 1.61e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 237667 [Multi-domain]  Cd Length: 291  Bit Score: 42.23  E-value: 1.61e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 112293277  59 FEVLQIDPEVTDEEIKKRFRQLSILVHPDKNQDDAdrAQKAFEAVDKAYKLLLDQEQKK 117
Cdd:PRK14299   7 YAILGVPKNASQDEIKKAFKKLARKYHPDVNKSPG--AEEKFKEINEAYTVLSDPEKRR 63
PRK14292 PRK14292
chaperone protein DnaJ; Provisional
 59-119 1.76e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 237662 [Multi-domain]  Cd Length: 371  Bit Score: 42.18  E-value: 1.76e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 112293277  59 FEVLQIDPEVTDEEIKKRFRQLSILVHPDKNQDDAdrAQKAFEAVDKAYKLLLDQEqkKRA 119
Cdd:PRK14292   5 YELLGVSRTASADEIKSAYRKLALKYHPDRNKEKG--AAEKFAQINEAYAVLSDAE--KRA 61
PRK14288 PRK14288
molecular chaperone DnaJ;
56-120 2.29e-04

molecular chaperone DnaJ;


Pssm-ID: 172776 [Multi-domain]  Cd Length: 369  Bit Score: 41.98  E-value: 2.29e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 112293277  56 LNPFEVLQIDPEVTDEEIKKRFRQLSILVHPDKNQDDADrAQKAFEAVDKAYKLLLDqeQKKRAL 120
Cdd:PRK14288   3 LSYYEILEVEKHSNQETIKKSYRKLALKYHPDRNAGDKE-AEEKFKLINEAYGVLSD--EKKRAL 64
PRK14296 PRK14296
chaperone protein DnaJ; Provisional
 59-118 4.14e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 237666 [Multi-domain]  Cd Length: 372  Bit Score: 41.09  E-value: 4.14e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293277  59 FEVLQIDPEVTDEEIKKRFRQLSILVHPDKNQDDAdrAQKAFEAVDKAYKLLLDQEQKKR 118
Cdd:PRK14296   7 YEVLGVSKTASEQEIRQAYRKLAKQYHPDLNKSPD--AHDKMVEINEAADVLLDKDKRKQ 64
PRK14300 PRK14300
chaperone protein DnaJ; Provisional
 59-121 4.56e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 172788 [Multi-domain]  Cd Length: 372  Bit Score: 40.77  E-value: 4.56e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 112293277  59 FEVLQIDPEVTDEEIKKRFRQLSILVHPDKNqdDADRAQKAFEAVDKAYKLLLDqEQKKRALD 121
Cdd:PRK14300   6 YQILGVSKTASQADLKKAYLKLAKQYHPDTT--DAKDAEKKFKEINAAYDVLKD-EQKRAAYD 65
PRK14293 PRK14293
molecular chaperone DnaJ;
59-118 9.55e-04

molecular chaperone DnaJ;


Pssm-ID: 237663 [Multi-domain]  Cd Length: 374  Bit Score: 39.97  E-value: 9.55e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 112293277  59 FEVLQIDPEVTDEEIKKRFRQLSILVHPDKNQDDAdrAQKAFEAVDKAYKLLLDQEQKKR 118
Cdd:PRK14293   6 YEILGVSRDADKDELKRAYRRLARKYHPDVNKEPG--AEDRFKEINRAYEVLSDPETRAR 63
 
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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