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Conserved domains on  [gi|118498347|ref|NP_001015882|]
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dnaJ homolog subfamily C member 25 precursor [Homo sapiens]

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 ...
 49-121 1.91e-22

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: 89.07  E-value: 1.91e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 118498347   49 DCYEVLGVSRSAGKAEIARAYRQLARRYHPDRYRPQPGdegpgrtpqsAEEAFLLVATAYETLKDEETRKDYD 121
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 ...
 49-121 1.91e-22

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: 89.07  E-value: 1.91e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 118498347   49 DCYEVLGVSRSAGKAEIARAYRQLARRYHPDRYRPQPGdegpgrtpqsAEEAFLLVATAYETLKDEETRKDYD 121
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNPGDPE----------AEEKFKEINEAYEVLSDPEKRAIYD 63
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 49-121 6.65e-21

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: 87.45  E-value: 6.65e-21
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 118498347  49 DCYEVLGVSRSAGKAEIARAYRQLARRYHPDRYrpqPGDEGpgrtpqsAEEAFLLVATAYETLKDEETRKDYD 121
Cdd:COG0484    1 DYYEILGVSRDASAEEIKKAYRKLAKKYHPDRN---PGDPE-------AEEKFKEINEAYEVLSDPEKRAAYD 63
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 48-121 3.56e-20

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 90.59  E-value: 3.56e-20
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 118498347  48 RDCYEVLGVSRSAGKAEIARAYRQLARRYHPDRyrpQPGDEgpgrtpqSAEEAFLLVATAYETLKDEETRKDYD 121
Cdd:PRK10767   4 RDYYEVLGVSRNASEDEIKKAYRKLAMKYHPDR---NPGDK-------EAEEKFKEIKEAYEVLSDPQKRAAYD 67
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
 49-121 1.38e-19

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: 88.43  E-value: 1.38e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 118498347   49 DCYEVLGVSRSAGKAEIARAYRQLARRYHPDRyRPQPGdegpgrtpqsAEEAFLLVATAYETLKDEETRKDYD 121
Cdd:TIGR02349   1 DYYEILGVSKDASEEEIKKAYRKLAKKYHPDR-NKDKE----------AEEKFKEINEAYEVLSDPEKRAQYD 62
DnaJ smart00271
DnaJ molecular chaperone homology domain;
48-115 1.93e-17

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 75.35  E-value: 1.93e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 118498347    48 RDCYEVLGVSRSAGKAEIARAYRQLARRYHPDRyrpqpgdegPGRTPQSAEEAFLLVATAYETLKDEE 115
Cdd:smart00271   1 TDYYEILGVPRDASLDEIKKAYRKLALKYHPDK---------NPGDKEEAEEKFKEINEAYEVLSDPE 59
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 49-113 1.33e-16

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


Pssm-ID: 99751 [Multi-domain]  Cd Length: 55  Bit Score: 72.96  E-value: 1.33e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 118498347  49 DCYEVLGVSRSAGKAEIARAYRQLARRYHPDRYRPQPGdegpgrtpqsAEEAFLLVATAYETLKD 113
Cdd:cd06257    1 DYYDILGVPPDASDEEIKKAYRKLALKYHPDKNPDDPE----------AEEKFKEINEAYEVLSD 55
terminal_TopJ NF037946
terminal organelle assembly protein TopJ;
48-121 3.17e-14

terminal organelle assembly protein TopJ;


Pssm-ID: 468284 [Multi-domain]  Cd Length: 440  Bit Score: 73.32  E-value: 3.17e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 118498347  48 RDCYEVLGVSRSAGKAEIARAYRQLARRYHPDRyrpqPGDEGpgrtpqsAEEAFLLVATAYETLKDEETRKDYD 121
Cdd:NF037946   5 RDYYEVLGVDRDADDQEIKKAFRKLAKKYHPDR----NKAPD-------AAEIFAEINEAYEVLSNPEKRANYD 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 ...
 49-121 1.91e-22

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: 89.07  E-value: 1.91e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 118498347   49 DCYEVLGVSRSAGKAEIARAYRQLARRYHPDRYRPQPGdegpgrtpqsAEEAFLLVATAYETLKDEETRKDYD 121
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNPGDPE----------AEEKFKEINEAYEVLSDPEKRAIYD 63
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 49-121 6.65e-21

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: 87.45  E-value: 6.65e-21
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 118498347  49 DCYEVLGVSRSAGKAEIARAYRQLARRYHPDRYrpqPGDEGpgrtpqsAEEAFLLVATAYETLKDEETRKDYD 121
Cdd:COG0484    1 DYYEILGVSRDASAEEIKKAYRKLAKKYHPDRN---PGDPE-------AEEKFKEINEAYEVLSDPEKRAAYD 63
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 48-121 3.56e-20

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 90.59  E-value: 3.56e-20
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 118498347  48 RDCYEVLGVSRSAGKAEIARAYRQLARRYHPDRyrpQPGDEgpgrtpqSAEEAFLLVATAYETLKDEETRKDYD 121
Cdd:PRK10767   4 RDYYEVLGVSRNASEDEIKKAYRKLAMKYHPDR---NPGDK-------EAEEKFKEIKEAYEVLSDPQKRAAYD 67
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
48-127 1.17e-19

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


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 82.46  E-value: 1.17e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118498347  48 RDCYEVLGVSRSAGKAEIARAYRQLARRYHPDRYrpqpgdegpGRTPQSAEEAFLLVATAYETLKDEETRKDYDYMLDHP 127
Cdd:COG2214    5 KDHYAVLGVPPDASLEEIRQAYRRLAKLLHPDRG---------GELKALAEELFQRLNEAYEVLSDPERRAEYDRELGQS 75
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
 49-121 1.38e-19

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: 88.43  E-value: 1.38e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 118498347   49 DCYEVLGVSRSAGKAEIARAYRQLARRYHPDRyRPQPGdegpgrtpqsAEEAFLLVATAYETLKDEETRKDYD 121
Cdd:TIGR02349   1 DYYEILGVSKDASEEEIKKAYRKLAKKYHPDR-NKDKE----------AEEKFKEINEAYEVLSDPEKRAQYD 62
PRK14293 PRK14293
molecular chaperone DnaJ;
48-121 5.49e-18

molecular chaperone DnaJ;


Pssm-ID: 237663 [Multi-domain]  Cd Length: 374  Bit Score: 84.27  E-value: 5.49e-18
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 118498347  48 RDCYEVLGVSRSAGKAEIARAYRQLARRYHPDRYRpQPGdegpgrtpqsAEEAFLLVATAYETLKDEETRKDYD 121
Cdd:PRK14293   3 ADYYEILGVSRDADKDELKRAYRRLARKYHPDVNK-EPG----------AEDRFKEINRAYEVLSDPETRARYD 65
DnaJ smart00271
DnaJ molecular chaperone homology domain;
48-115 1.93e-17

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 75.35  E-value: 1.93e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 118498347    48 RDCYEVLGVSRSAGKAEIARAYRQLARRYHPDRyrpqpgdegPGRTPQSAEEAFLLVATAYETLKDEE 115
Cdd:smart00271   1 TDYYEILGVPRDASLDEIKKAYRKLALKYHPDK---------NPGDKEEAEEKFKEINEAYEVLSDPE 59
PRK14301 PRK14301
chaperone protein DnaJ; Provisional
 48-121 3.20e-17

chaperone protein DnaJ; Provisional


Pssm-ID: 237668 [Multi-domain]  Cd Length: 373  Bit Score: 82.10  E-value: 3.20e-17
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 118498347  48 RDCYEVLGVSRSAGKAEIARAYRQLARRYHPDRyrpQPGDegpgrtpQSAEEAFLLVATAYETLKDEETRKDYD 121
Cdd:PRK14301   4 RDYYEVLGVSRDASEDEIKKAYRKLALQYHPDR---NPDN-------PEAEQKFKEAAEAYEVLRDAEKRARYD 67
PRK14280 PRK14280
molecular chaperone DnaJ;
48-121 5.26e-17

molecular chaperone DnaJ;


Pssm-ID: 237656 [Multi-domain]  Cd Length: 376  Bit Score: 81.31  E-value: 5.26e-17
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 118498347  48 RDCYEVLGVSRSAGKAEIARAYRQLARRYHPDRYRpqpgDEGpgrtpqsAEEAFLLVATAYETLKDEETRKDYD 121
Cdd:PRK14280   4 RDYYEVLGVSKSASKDEIKKAYRKLSKKYHPDINK----EEG-------ADEKFKEISEAYEVLSDDQKRAQYD 66
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 49-113 1.33e-16

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


Pssm-ID: 99751 [Multi-domain]  Cd Length: 55  Bit Score: 72.96  E-value: 1.33e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 118498347  49 DCYEVLGVSRSAGKAEIARAYRQLARRYHPDRYRPQPGdegpgrtpqsAEEAFLLVATAYETLKD 113
Cdd:cd06257    1 DYYDILGVPPDASDEEIKKAYRKLALKYHPDKNPDDPE----------AEEKFKEINEAYEVLSD 55
PRK14281 PRK14281
chaperone protein DnaJ; Provisional
 48-121 2.10e-16

chaperone protein DnaJ; Provisional


Pssm-ID: 237657 [Multi-domain]  Cd Length: 397  Bit Score: 79.85  E-value: 2.10e-16
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 118498347  48 RDCYEVLGVSRSAGKAEIARAYRQLARRYHPDRyrpQPGDegpgrtpQSAEEAFLLVATAYETLKDEETRKDYD 121
Cdd:PRK14281   3 RDYYEVLGVSRSADKDEIKKAYRKLALKYHPDK---NPDN-------KEAEEHFKEVNEAYEVLSNDDKRRRYD 66
SEC63 COG5407
Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular ...
 49-118 2.14e-16

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


Pssm-ID: 444165 [Multi-domain]  Cd Length: 61  Bit Score: 72.72  E-value: 2.14e-16
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118498347  49 DCYEVLGVSRSAGKAEIARAYRQLARRYHPDRyrpQPGDEGpgrtpqsAEEAFLLVATAYETLKDEETRK 118
Cdd:COG5407    1 DPYEVLGVAKTASADEIKKAYRKLAKKYHPDR---NKGDPK-------AEERFKEINEAYELLSDAEKRA 60
PRK14294 PRK14294
chaperone protein DnaJ; Provisional
 46-121 3.91e-16

chaperone protein DnaJ; Provisional


Pssm-ID: 237664 [Multi-domain]  Cd Length: 366  Bit Score: 78.65  E-value: 3.91e-16
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 118498347  46 GTRDCYEVLGVSRSAGKAEIARAYRQLARRYHPDRyrpQPGDegpgrtpQSAEEAFLLVATAYETLKDEETRKDYD 121
Cdd:PRK14294   2 VKRDYYEILGVTRDASEEEIKKSYRKLAMKYHPDR---NPGD-------KEAEELFKEAAEAYEVLSDPKKRGIYD 67
PRK14291 PRK14291
chaperone protein DnaJ; Provisional
 48-121 6.52e-16

chaperone protein DnaJ; Provisional


Pssm-ID: 237661 [Multi-domain]  Cd Length: 382  Bit Score: 78.27  E-value: 6.52e-16
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 118498347  48 RDCYEVLGVSRSAGKAEIARAYRQLARRYHPDrYRPQPGdegpgrtpqsAEEAFLLVATAYETLKDEETRKDYD 121
Cdd:PRK14291   3 KDYYEILGVSRNATQEEIKKAYRRLARKYHPD-FNKNPE----------AEEKFKEINEAYQVLSDPEKRKLYD 65
PRK14277 PRK14277
chaperone protein DnaJ; Provisional
 46-121 7.51e-16

chaperone protein DnaJ; Provisional


Pssm-ID: 184599 [Multi-domain]  Cd Length: 386  Bit Score: 77.92  E-value: 7.51e-16
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 118498347  46 GTRDCYEVLGVSRSAGKAEIARAYRQLARRYHPDRyrpQPGDegpgrtpQSAEEAFLLVATAYETLKDEETRKDYD 121
Cdd:PRK14277   3 AKKDYYEILGVDRNATEEEIKKAYRRLAKKYHPDL---NPGD-------KEAEQKFKEINEAYEILSDPQKRAQYD 68
PRK14283 PRK14283
chaperone protein DnaJ; Provisional
 48-121 1.89e-15

chaperone protein DnaJ; Provisional


Pssm-ID: 184604 [Multi-domain]  Cd Length: 378  Bit Score: 76.79  E-value: 1.89e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 118498347  48 RDCYEVLGVSRSAGKAEIARAYRQLARRYHPDRYRpqpgDEGpgrtpqsAEEAFLLVATAYETLKDEETRKDYD 121
Cdd:PRK14283   5 RDYYEVLGVDRNADKKEIKKAYRKLARKYHPDVSE----EEG-------AEEKFKEISEAYAVLSDDEKRQRYD 67
PRK14276 PRK14276
chaperone protein DnaJ; Provisional
 48-121 2.16e-15

chaperone protein DnaJ; Provisional


Pssm-ID: 237653 [Multi-domain]  Cd Length: 380  Bit Score: 76.67  E-value: 2.16e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 118498347  48 RDCYEVLGVSRSAGKAEIARAYRQLARRYHPDrYRPQPGdegpgrtpqsAEEAFLLVATAYETLKDEETRKDYD 121
Cdd:PRK14276   4 TEYYDRLGVSKDASQDEIKKAYRKLSKKYHPD-INKEPG----------AEEKYKEVQEAYETLSDPQKRAAYD 66
PRK14279 PRK14279
molecular chaperone DnaJ;
48-121 2.67e-15

molecular chaperone DnaJ;


Pssm-ID: 237655 [Multi-domain]  Cd Length: 392  Bit Score: 76.31  E-value: 2.67e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 118498347  48 RDCYEVLGVSRSAGKAEIARAYRQLARRYHPDRyrpQPGDegpgrtpQSAEEAFLLVATAYETLKDEETRKDYD 121
Cdd:PRK14279   9 KDFYKELGVSSDASAEEIKKAYRKLARELHPDA---NPGD-------PAAEERFKAVSEAHDVLSDPAKRKEYD 72
PRK14295 PRK14295
molecular chaperone DnaJ;
48-121 6.19e-15

molecular chaperone DnaJ;


Pssm-ID: 237665 [Multi-domain]  Cd Length: 389  Bit Score: 75.27  E-value: 6.19e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 118498347  48 RDCYEVLGVSRSAGKAEIARAYRQLARRYHPDRYRPQPGdegpgrtpqsAEEAFLLVATAYETLKDEETRKDYD 121
Cdd:PRK14295   9 KDYYKVLGVPKDATEAEIKKAYRKLAREYHPDANKGDAK----------AEERFKEISEAYDVLSDEKKRKEYD 72
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
 47-121 1.95e-14

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 73.73  E-value: 1.95e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 118498347  47 TRDCYEVLGVSRSAGKAEIARAYRQLARRYHPDRYRpQPGdegpgrtpqsAEEAFLLVATAYETLKDEETRKDYD 121
Cdd:PRK14298   4 TRDYYEILGLSKDASVEDIKKAYRKLAMKYHPDKNK-EPD----------AEEKFKEISEAYAVLSDAEKRAQYD 67
PRK14278 PRK14278
chaperone protein DnaJ; Provisional
 48-121 2.81e-14

chaperone protein DnaJ; Provisional


Pssm-ID: 237654 [Multi-domain]  Cd Length: 378  Bit Score: 73.16  E-value: 2.81e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 118498347  48 RDCYEVLGVSRSAGKAEIARAYRQLARRYHPDryrPQPGDEgpgrtpqsAEEAFLLVATAYETLKDEETRKDYD 121
Cdd:PRK14278   3 RDYYGLLGVSRNASDAEIKRAYRKLARELHPD---VNPDEE--------AQEKFKEISVAYEVLSDPEKRRIVD 65
terminal_TopJ NF037946
terminal organelle assembly protein TopJ;
48-121 3.17e-14

terminal organelle assembly protein TopJ;


Pssm-ID: 468284 [Multi-domain]  Cd Length: 440  Bit Score: 73.32  E-value: 3.17e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 118498347  48 RDCYEVLGVSRSAGKAEIARAYRQLARRYHPDRyrpqPGDEGpgrtpqsAEEAFLLVATAYETLKDEETRKDYD 121
Cdd:NF037946   5 RDYYEVLGVDRDADDQEIKKAFRKLAKKYHPDR----NKAPD-------AAEIFAEINEAYEVLSNPEKRANYD 67
PRK14289 PRK14289
molecular chaperone DnaJ;
48-121 1.39e-13

molecular chaperone DnaJ;


Pssm-ID: 237660 [Multi-domain]  Cd Length: 386  Bit Score: 71.02  E-value: 1.39e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 118498347  48 RDCYEVLGVSRSAGKAEIARAYRQLARRYHPDRyrpQPGDegpgrtpQSAEEAFLLVATAYETLKDEETRKDYD 121
Cdd:PRK14289   5 RDYYEVLGVSKTATVDEIKKAYRKKAIQYHPDK---NPGD-------KEAEEKFKEAAEAYDVLSDPDKRSRYD 68
PRK14284 PRK14284
chaperone protein DnaJ; Provisional
 49-121 2.07e-13

chaperone protein DnaJ; Provisional


Pssm-ID: 237658 [Multi-domain]  Cd Length: 391  Bit Score: 70.64  E-value: 2.07e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 118498347  49 DCYEVLGVSRSAGKAEIARAYRQLARRYHPDRyrpQPGDegpgrtpQSAEEAFLLVATAYETLKDEETRKDYD 121
Cdd:PRK14284   2 DYYTILGVSKTASPEEIKKAYRKLAVKYHPDK---NPGD-------AEAEKRFKEVSEAYEVLSDAQKRESYD 64
PRK14290 PRK14290
chaperone protein DnaJ; Provisional
 48-121 5.50e-13

chaperone protein DnaJ; Provisional


Pssm-ID: 172778 [Multi-domain]  Cd Length: 365  Bit Score: 69.19  E-value: 5.50e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 118498347  48 RDCYEVLGVSRSAGKAEIARAYRQLARRYHPDRYrpqPGDEgpgrtpQSAEEAFLLVATAYETLKDEETRKDYD 121
Cdd:PRK14290   3 KDYYKILGVDRNASQEDIKKAFRELAKKWHPDLH---PGNK------AEAEEKFKEISEAYEVLSDPQKRRQYD 67
PRK14292 PRK14292
chaperone protein DnaJ; Provisional
 49-121 5.94e-13

chaperone protein DnaJ; Provisional


Pssm-ID: 237662 [Multi-domain]  Cd Length: 371  Bit Score: 69.15  E-value: 5.94e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 118498347  49 DCYEVLGVSRSAGKAEIARAYRQLARRYHPDRyRPQPGdegpgrtpqsAEEAFLLVATAYETLKDEETRKDYD 121
Cdd:PRK14292   3 DYYELLGVSRTASADEIKSAYRKLALKYHPDR-NKEKG----------AAEKFAQINEAYAVLSDAEKRAHYD 64
PRK14297 PRK14297
molecular chaperone DnaJ;
48-121 8.22e-13

molecular chaperone DnaJ;


Pssm-ID: 184611 [Multi-domain]  Cd Length: 380  Bit Score: 68.66  E-value: 8.22e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 118498347  48 RDCYEVLGVSRSAGKAEIARAYRQLARRYHPDRyrpQPGDegpgrtpQSAEEAFLLVATAYETLKDEETRKDYD 121
Cdd:PRK14297   4 KDYYEVLGLEKGASDDEIKKAFRKLAIKYHPDK---NKGN-------KEAEEKFKEINEAYQVLSDPQKKAQYD 67
PRK14286 PRK14286
chaperone protein DnaJ; Provisional
 48-121 2.82e-12

chaperone protein DnaJ; Provisional


Pssm-ID: 172774 [Multi-domain]  Cd Length: 372  Bit Score: 67.32  E-value: 2.82e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 118498347  48 RDCYEVLGVSRSAGKAEIARAYRQLARRYHPDRYRpqpGDegpgrtpQSAEEAFLLVATAYETLKDEETRKDYD 121
Cdd:PRK14286   4 RSYYDILGVSKSANDEEIKSAYRKLAIKYHPDKNK---GN-------KESEEKFKEATEAYEILRDPKKRQAYD 67
PRK14282 PRK14282
chaperone protein DnaJ; Provisional
 48-121 3.21e-12

chaperone protein DnaJ; Provisional


Pssm-ID: 184603 [Multi-domain]  Cd Length: 369  Bit Score: 67.13  E-value: 3.21e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 118498347  48 RDCYEVLGVSRSAGKAEIARAYRQLARRYHPDRYrpqPGDEgpgrtpQSAEEAFLLVATAYETLKDEETRKDYD 121
Cdd:PRK14282   4 KDYYEILGVSRNATQEEIKRAYKRLVKEWHPDRH---PENR------KEAEQKFKEIQEAYEVLSDPQKRAMYD 68
PRK10266 PRK10266
curved DNA-binding protein;
48-126 3.61e-12

curved DNA-binding protein;


Pssm-ID: 182347 [Multi-domain]  Cd Length: 306  Bit Score: 66.38  E-value: 3.61e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 118498347  48 RDCYEVLGVSRSAGKAEIARAYRQLARRYHPDRyrpqpgdegpgRTPQSAEEAFLLVATAYETLKDEETRKDYDYMLDH 126
Cdd:PRK10266   4 KDYYAIMGVKPTDDLKTIKTAYRRLARKYHPDV-----------SKEPDAEARFKEVAEAWEVLSDEQRRAEYDQLWQH 71
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
46-114 8.72e-12

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


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 60.20  E-value: 8.72e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 118498347  46 GTRDCYEVLGVSRSAGKAEIARAYRQLARRYHPDRYRpqpgdegpgrtpQSAEEAFLLVAT--------AYETLKDE 114
Cdd:COG1076    2 QLDDAFELLGLPPDADDAELKRAYRKLQREHHPDRLA------------AGLPEEEQRLALqkaaaineAYETLKDP 66
PRK14287 PRK14287
chaperone protein DnaJ; Provisional
 48-121 1.22e-11

chaperone protein DnaJ; Provisional


Pssm-ID: 237659 [Multi-domain]  Cd Length: 371  Bit Score: 65.03  E-value: 1.22e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 118498347  48 RDCYEVLGVSRSAGKAEIARAYRQLARRYHPDRYRpqpgdegpgrtPQSAEEAFLLVATAYETLKDEETRKDYD 121
Cdd:PRK14287   4 RDYYEVLGVDRNASVDEVKKAYRKLARKYHPDVNK-----------APDAEDKFKEVKEAYDTLSDPQKKAHYD 66
PRK14299 PRK14299
chaperone protein DnaJ; Provisional
 48-121 1.44e-11

chaperone protein DnaJ; Provisional


Pssm-ID: 237667 [Multi-domain]  Cd Length: 291  Bit Score: 64.19  E-value: 1.44e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 118498347  48 RDCYEVLGVSRSAGKAEIARAYRQLARRYHPDRyrpqpgDEGPGrtpqsAEEAFLLVATAYETLKDEETRKDYD 121
Cdd:PRK14299   4 KDYYAILGVPKNASQDEIKKAFKKLARKYHPDV------NKSPG-----AEEKFKEINEAYTVLSDPEKRRIYD 66
PRK14300 PRK14300
chaperone protein DnaJ; Provisional
 47-121 1.58e-11

chaperone protein DnaJ; Provisional


Pssm-ID: 172788 [Multi-domain]  Cd Length: 372  Bit Score: 65.04  E-value: 1.58e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 118498347  47 TRDCYEVLGVSRSAGKAEIARAYRQLARRYHPDryRPQPGDegpgrtpqsAEEAFLLVATAYETLKDEETRKDYD 121
Cdd:PRK14300   2 SQDYYQILGVSKTASQADLKKAYLKLAKQYHPD--TTDAKD---------AEKKFKEINAAYDVLKDEQKRAAYD 65
PRK14285 PRK14285
chaperone protein DnaJ; Provisional
 48-121 5.13e-11

chaperone protein DnaJ; Provisional


Pssm-ID: 172773 [Multi-domain]  Cd Length: 365  Bit Score: 63.47  E-value: 5.13e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 118498347  48 RDCYEVLGVSRSAGKAEIARAYRQLARRYHPDRyrpqpgdegpGRTPQSAEEAFLLVATAYETLKDEETRKDYD 121
Cdd:PRK14285   3 RDYYEILGLSKGASKDEIKKAYRKIAIKYHPDK----------NKGNKEAESIFKEATEAYEVLIDDNKRAQYD 66
PRK14296 PRK14296
chaperone protein DnaJ; Provisional
 48-121 7.34e-11

chaperone protein DnaJ; Provisional


Pssm-ID: 237666 [Multi-domain]  Cd Length: 372  Bit Score: 62.66  E-value: 7.34e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 118498347  48 RDCYEVLGVSRSAGKAEIARAYRQLARRYHPDRYRpQPGdegpgrtpqsAEEAFLLVATAYETLKDEETRKDYD 121
Cdd:PRK14296   4 KDYYEVLGVSKTASEQEIRQAYRKLAKQYHPDLNK-SPD----------AHDKMVEINEAADVLLDKDKRKQYD 66
PTZ00037 PTZ00037
DnaJ_C chaperone protein; Provisional
 51-121 4.70e-10

DnaJ_C chaperone protein; Provisional


Pssm-ID: 240236 [Multi-domain]  Cd Length: 421  Bit Score: 60.60  E-value: 4.70e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 118498347  51 YEVLGVSRSAGKAEIARAYRQLARRYHPDRyrpqPGDegpgrtpqsaEEAFLLVATAYETLKDEETRKDYD 121
Cdd:PTZ00037  31 YEVLNLSKDCTTSEIKKAYRKLAIKHHPDK----GGD----------PEKFKEISRAYEVLSDPEKRKIYD 87
PRK14288 PRK14288
molecular chaperone DnaJ;
51-121 1.91e-07

molecular chaperone DnaJ;


Pssm-ID: 172776 [Multi-domain]  Cd Length: 369  Bit Score: 52.38  E-value: 1.91e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 118498347  51 YEVLGVSRSAGKAEIARAYRQLARRYHPDRyrpQPGDegpgrtpQSAEEAFLLVATAYETLKDEETRKDYD 121
Cdd:PRK14288   6 YEILEVEKHSNQETIKKSYRKLALKYHPDR---NAGD-------KEAEEKFKLINEAYGVLSDEKKRALYD 66
djlA PRK09430
co-chaperone DjlA;
49-79 5.52e-07

co-chaperone DjlA;


Pssm-ID: 236512 [Multi-domain]  Cd Length: 267  Bit Score: 50.20  E-value: 5.52e-07
                         10        20        30
                 ....*....|....*....|....*....|.
gi 118498347  49 DCYEVLGVSRSAGKAEIARAYRQLARRYHPD 79
Cdd:PRK09430 201 DAYKVLGVSESDDDQEIKRAYRKLMSEHHPD 231
TetR_C_33 pfam13305
Tetracyclin repressor-like, C-terminal domain; This domain is around 80 amino acids in length. ...
 63-107 5.14e-04

Tetracyclin repressor-like, C-terminal domain; This domain is around 80 amino acids in length. It is found to the C-terminus of a DNA-binding helix-turn-helix domain. This domain may be involved transcriptional regulation predicted to belong to the TetR family. This domain contains three conserved residues (WHG) near the C-terminus.


Pssm-ID: 463838  Cd Length: 104  Bit Score: 39.19  E-value: 5.14e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 118498347   63 AEIARAYRQLARRyHPDRYR-----PQPGDEGPGRTPQSAEEAFLLVATA 107
Cdd:pfam13305   2 RALARAYRDFALA-HPGRYAlmfgsPVPGYLDPEELAAAGARVVALLLAV 50
ZUO1 COG5269
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ...
 46-121 5.48e-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: 5.48e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 118498347  46 GTRDCYEVLGVSRSAGKA---EIARAYRQLARRYHPDRyRPQPGDEGpgrtpqsAEEAFLLVATAYETLKDEETRKDYD 121
Cdd:COG5269   41 KKVDLYALLGLSKYRTKAippQILKAHKKKVYKYHPDK-TAAGGNKG-------CDEFFKLIQKAREVLGDRKLRLQYD 111
hscB PRK00294
co-chaperone HscB; Provisional
 63-120 4.76e-03

co-chaperone HscB; Provisional


Pssm-ID: 166894 [Multi-domain]  Cd Length: 173  Bit Score: 37.52  E-value: 4.76e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 118498347  63 AEIARAYRQLARRYHPDRYRpqpgdEGPGRTPQSAEEAFLLVATAYETLKDEETRKDY 120
Cdd:PRK00294  21 DQLATRYRELAREVHPDRFA-----DAPEREQRLALERSASLNEAYQTLKSPPRRARY 73
 
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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