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Conserved domains on  [gi|161760675|ref|NP_446142|]
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dnaJ homolog subfamily C member 14 [Rattus norvegicus]

Protein Classification

DnaJ homolog subfamily C member 14( domain architecture ID 10446388)

DnaJ homolog subfamily C member 14 (DNAJC14) regulates the export of target proteins, such as dopamine D1 receptor (DRD1), from the endoplasmic reticulum to the cell surface

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Jiv90 pfam14901
Cleavage inducing molecular chaperone; Jiv90 is a fragment of the DnaJ protein in eukaryotes ...
533-621 5.70e-46

Cleavage inducing molecular chaperone; Jiv90 is a fragment of the DnaJ protein in eukaryotes and in J-domain protein interacting with viral protein (Jiv) located in the N terminal region of the pestivirus viral polypeptide. The viral protein interacts stably with non structural (NS) protein NS2, causing a conformational change in NS2-NS3 and stimulates NS2-NS3 cleavage in trans. Cleavage of NS2-NS3 increases cytopathogenicity and consequently aids viral replication. Jiv therefore acts as a regulating cofactor for NS2 auto-protease. The efficient release of NS3 from the viral polypeptide by Jiv is considered crucial to the pestivirus cytopathogenicity. In eukaryotes, it usually lies 40 residues downstream of DnaJ family pfam00226. However, the function in eukaryotes is still unknown.


:

Pssm-ID: 464360  Cd Length: 92  Bit Score: 158.28  E-value: 5.70e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161760675  533 MNTMMCSRCQGKHRRFEMDREPKSARYCAECNRLHPAEEGDFWAESSMLGLKITYFALMDGKVYDITEWAGCQR---VGI 609
Cdd:pfam14901   1 ANTIRCTKCGNRHKRICTDRPKYAARWCQECKIFHSAKDGDIWVESSMLGLLWRYYACMDGKVYDITEWAICQGdslMHC 80
                          90
                  ....*....|..
gi 161760675  610 SPDTHRVPYHIS 621
Cdd:pfam14901  81 RPNTHRVQYRIN 92
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
444-505 1.21e-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: 91.38  E-value: 1.21e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 161760675  444 NPFHVLGVEATASDIELKKAYRQLAVMVHPDKN-HHPRAEEAFKVLRAAWDIVSNPERRKEYE 505
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNpGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
 
Name Accession Description Interval E-value
Jiv90 pfam14901
Cleavage inducing molecular chaperone; Jiv90 is a fragment of the DnaJ protein in eukaryotes ...
533-621 5.70e-46

Cleavage inducing molecular chaperone; Jiv90 is a fragment of the DnaJ protein in eukaryotes and in J-domain protein interacting with viral protein (Jiv) located in the N terminal region of the pestivirus viral polypeptide. The viral protein interacts stably with non structural (NS) protein NS2, causing a conformational change in NS2-NS3 and stimulates NS2-NS3 cleavage in trans. Cleavage of NS2-NS3 increases cytopathogenicity and consequently aids viral replication. Jiv therefore acts as a regulating cofactor for NS2 auto-protease. The efficient release of NS3 from the viral polypeptide by Jiv is considered crucial to the pestivirus cytopathogenicity. In eukaryotes, it usually lies 40 residues downstream of DnaJ family pfam00226. However, the function in eukaryotes is still unknown.


Pssm-ID: 464360  Cd Length: 92  Bit Score: 158.28  E-value: 5.70e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161760675  533 MNTMMCSRCQGKHRRFEMDREPKSARYCAECNRLHPAEEGDFWAESSMLGLKITYFALMDGKVYDITEWAGCQR---VGI 609
Cdd:pfam14901   1 ANTIRCTKCGNRHKRICTDRPKYAARWCQECKIFHSAKDGDIWVESSMLGLLWRYYACMDGKVYDITEWAICQGdslMHC 80
                          90
                  ....*....|..
gi 161760675  610 SPDTHRVPYHIS 621
Cdd:pfam14901  81 RPNTHRVQYRIN 92
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
444-505 1.21e-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: 91.38  E-value: 1.21e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 161760675  444 NPFHVLGVEATASDIELKKAYRQLAVMVHPDKN-HHPRAEEAFKVLRAAWDIVSNPERRKEYE 505
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNpGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
444-516 3.62e-20

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: 87.07  E-value: 3.62e-20
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 161760675 444 NPFHVLGVEATASDIELKKAYRQLAVMVHPDKNH-HPRAEEAFKVLRAAWDIVSNPERRKEYEMKRMAENELSR 516
Cdd:COG0484    1 DYYEILGVSRDASAEEIKKAYRKLAKKYHPDRNPgDPEAEEKFKEINEAYEVLSDPEKRAAYDRFGHAAELLLA 74
DnaJ smart00271
DnaJ molecular chaperone homology domain;
444-500 1.48e-17

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 76.89  E-value: 1.48e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 161760675   444 NPFHVLGVEATASDIELKKAYRQLAVMVHPDKN--HHPRAEEAFKVLRAAWDIVSNPER 500
Cdd:smart00271   2 DYYEILGVPRDASLDEIKKAYRKLALKYHPDKNpgDKEEAEEKFKEINEAYEVLSDPEK 60
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
444-497 1.54e-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: 74.12  E-value: 1.54e-16
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 161760675 444 NPFHVLGVEATASDIELKKAYRQLAVMVHPDKN-HHPRAEEAFKVLRAAWDIVSN 497
Cdd:cd06257    1 DYYDILGVPPDASDEEIKKAYRKLALKYHPDKNpDDPEAEEKFKEINEAYEVLSD 55
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
448-504 4.12e-15

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: 77.26  E-value: 4.12e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 161760675  448 VLGVEATASDIELKKAYRQLAVMVHPDKNHHPRAEEAFKVLRAAWDIVSNPERRKEY 504
Cdd:TIGR02349   5 ILGVSKDASEEEIKKAYRKLAKKYHPDRNKDKEAEEKFKEINEAYEVLSDPEKRAQY 61
PRK14295 PRK14295
molecular chaperone DnaJ;
446-508 5.57e-14

molecular chaperone DnaJ;


Pssm-ID: 237665 [Multi-domain]  Cd Length: 389  Bit Score: 74.11  E-value: 5.57e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 161760675 446 FHVLGVEATASDIELKKAYRQLAVMVHPDKNH-HPRAEEAFKVLRAAWDIVSNPERRKEYEMKR 508
Cdd:PRK14295  12 YKVLGVPKDATEAEIKKAYRKLAREYHPDANKgDAKAEERFKEISEAYDVLSDEKKRKEYDEAR 75
terminal_TopJ NF037946
terminal organelle assembly protein TopJ;
446-505 1.45e-11

terminal organelle assembly protein TopJ;


Pssm-ID: 468284 [Multi-domain]  Cd Length: 440  Bit Score: 67.15  E-value: 1.45e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 161760675 446 FHVLGVEATASDIELKKAYRQLAVMVHPDKNHHPRAEEAFKVLRAAWDIVSNPERRKEYE 505
Cdd:NF037946   8 YEVLGVDRDADDQEIKKAFRKLAKKYHPDRNKAPDAAEIFAEINEAYEVLSNPEKRANYD 67
 
Name Accession Description Interval E-value
Jiv90 pfam14901
Cleavage inducing molecular chaperone; Jiv90 is a fragment of the DnaJ protein in eukaryotes ...
533-621 5.70e-46

Cleavage inducing molecular chaperone; Jiv90 is a fragment of the DnaJ protein in eukaryotes and in J-domain protein interacting with viral protein (Jiv) located in the N terminal region of the pestivirus viral polypeptide. The viral protein interacts stably with non structural (NS) protein NS2, causing a conformational change in NS2-NS3 and stimulates NS2-NS3 cleavage in trans. Cleavage of NS2-NS3 increases cytopathogenicity and consequently aids viral replication. Jiv therefore acts as a regulating cofactor for NS2 auto-protease. The efficient release of NS3 from the viral polypeptide by Jiv is considered crucial to the pestivirus cytopathogenicity. In eukaryotes, it usually lies 40 residues downstream of DnaJ family pfam00226. However, the function in eukaryotes is still unknown.


Pssm-ID: 464360  Cd Length: 92  Bit Score: 158.28  E-value: 5.70e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161760675  533 MNTMMCSRCQGKHRRFEMDREPKSARYCAECNRLHPAEEGDFWAESSMLGLKITYFALMDGKVYDITEWAGCQR---VGI 609
Cdd:pfam14901   1 ANTIRCTKCGNRHKRICTDRPKYAARWCQECKIFHSAKDGDIWVESSMLGLLWRYYACMDGKVYDITEWAICQGdslMHC 80
                          90
                  ....*....|..
gi 161760675  610 SPDTHRVPYHIS 621
Cdd:pfam14901  81 RPNTHRVQYRIN 92
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
444-505 1.21e-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: 91.38  E-value: 1.21e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 161760675  444 NPFHVLGVEATASDIELKKAYRQLAVMVHPDKN-HHPRAEEAFKVLRAAWDIVSNPERRKEYE 505
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNpGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
444-516 3.62e-20

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: 87.07  E-value: 3.62e-20
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 161760675 444 NPFHVLGVEATASDIELKKAYRQLAVMVHPDKNH-HPRAEEAFKVLRAAWDIVSNPERRKEYEMKRMAENELSR 516
Cdd:COG0484    1 DYYEILGVSRDASAEEIKKAYRKLAKKYHPDRNPgDPEAEEKFKEINEAYEVLSDPEKRAAYDRFGHAAELLLA 74
SEC63 COG5407
Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular ...
444-503 2.44e-19

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


Pssm-ID: 444165 [Multi-domain]  Cd Length: 61  Bit Score: 81.97  E-value: 2.44e-19
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 161760675 444 NPFHVLGVEATASDIELKKAYRQLAVMVHPDKN-HHPRAEEAFKVLRAAWDIVSNPERRKE 503
Cdd:COG5407    1 DPYEVLGVAKTASADEIKKAYRKLAKKYHPDRNkGDPKAEERFKEINEAYELLSDAEKRAR 61
DnaJ smart00271
DnaJ molecular chaperone homology domain;
444-500 1.48e-17

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 76.89  E-value: 1.48e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 161760675   444 NPFHVLGVEATASDIELKKAYRQLAVMVHPDKN--HHPRAEEAFKVLRAAWDIVSNPER 500
Cdd:smart00271   2 DYYEILGVPRDASLDEIKKAYRKLALKYHPDKNpgDKEEAEEKFKEINEAYEVLSDPEK 60
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
441-504 7.97e-17

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


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 75.91  E-value: 7.97e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 161760675 441 DELNPFHVLGVEATASDIELKKAYRQLAVMVHPDKN--HHPRAEEAFKVLRAAWDIVSNPERRKEY 504
Cdd:COG2214    3 DLKDHYAVLGVPPDASLEEIRQAYRRLAKLLHPDRGgeLKALAEELFQRLNEAYEVLSDPERRAEY 68
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
444-497 1.54e-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: 74.12  E-value: 1.54e-16
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 161760675 444 NPFHVLGVEATASDIELKKAYRQLAVMVHPDKN-HHPRAEEAFKVLRAAWDIVSN 497
Cdd:cd06257    1 DYYDILGVPPDASDEEIKKAYRKLALKYHPDKNpDDPEAEEKFKEINEAYEVLSD 55
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
448-504 4.12e-15

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: 77.26  E-value: 4.12e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 161760675  448 VLGVEATASDIELKKAYRQLAVMVHPDKNHHPRAEEAFKVLRAAWDIVSNPERRKEY 504
Cdd:TIGR02349   5 ILGVSKDASEEEIKKAYRKLAKKYHPDRNKDKEAEEKFKEINEAYEVLSDPEKRAQY 61
PRK14295 PRK14295
molecular chaperone DnaJ;
446-508 5.57e-14

molecular chaperone DnaJ;


Pssm-ID: 237665 [Multi-domain]  Cd Length: 389  Bit Score: 74.11  E-value: 5.57e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 161760675 446 FHVLGVEATASDIELKKAYRQLAVMVHPDKNH-HPRAEEAFKVLRAAWDIVSNPERRKEYEMKR 508
Cdd:PRK14295  12 YKVLGVPKDATEAEIKKAYRKLAREYHPDANKgDAKAEERFKEISEAYDVLSDEKKRKEYDEAR 75
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
446-505 1.77e-13

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 72.57  E-value: 1.77e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 161760675 446 FHVLGVEATASDIELKKAYRQLAVMVHPDKNHHPRAEEAFKVLRAAWDIVSNPERRKEYE 505
Cdd:PRK14298   8 YEILGLSKDASVEDIKKAYRKLAMKYHPDKNKEPDAEEKFKEISEAYAVLSDAEKRAQYD 67
PRK14291 PRK14291
chaperone protein DnaJ; Provisional
446-506 3.03e-13

chaperone protein DnaJ; Provisional


Pssm-ID: 237661 [Multi-domain]  Cd Length: 382  Bit Score: 72.11  E-value: 3.03e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 161760675 446 FHVLGVEATASDIELKKAYRQLAVMVHPDKNHHPRAEEAFKVLRAAWDIVSNPERRKEYEM 506
Cdd:PRK14291   6 YEILGVSRNATQEEIKKAYRRLARKYHPDFNKNPEAEEKFKEINEAYQVLSDPEKRKLYDQ 66
PRK14289 PRK14289
molecular chaperone DnaJ;
446-505 3.15e-13

molecular chaperone DnaJ;


Pssm-ID: 237660 [Multi-domain]  Cd Length: 386  Bit Score: 71.79  E-value: 3.15e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 161760675 446 FHVLGVEATASDIELKKAYRQLAVMVHPDKNHHPR-AEEAFKVLRAAWDIVSNPERRKEYE 505
Cdd:PRK14289   8 YEVLGVSKTATVDEIKKAYRKKAIQYHPDKNPGDKeAEEKFKEAAEAYDVLSDPDKRSRYD 68
PRK14279 PRK14279
molecular chaperone DnaJ;
449-509 6.03e-13

molecular chaperone DnaJ;


Pssm-ID: 237655 [Multi-domain]  Cd Length: 392  Bit Score: 71.30  E-value: 6.03e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 161760675 449 LGVEATASDIELKKAYRQLAVMVHPDKN-HHPRAEEAFKVLRAAWDIVSNPERRKEY-EMKRM 509
Cdd:PRK14279  15 LGVSSDASAEEIKKAYRKLARELHPDANpGDPAAEERFKAVSEAHDVLSDPAKRKEYdETRRL 77
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
448-504 9.09e-13

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 70.17  E-value: 9.09e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 161760675 448 VLGVEATASDIELKKAYRQLAVMVHPDKNH-HPRAEEAFKVLRAAWDIVSNPERRKEY 504
Cdd:PRK10767   9 VLGVSRNASEDEIKKAYRKLAMKYHPDRNPgDKEAEEKFKEIKEAYEVLSDPQKRAAY 66
PRK14283 PRK14283
chaperone protein DnaJ; Provisional
446-519 1.01e-12

chaperone protein DnaJ; Provisional


Pssm-ID: 184604 [Multi-domain]  Cd Length: 378  Bit Score: 70.24  E-value: 1.01e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161760675 446 FHVLGVEATASDIELKKAYRQLAVMVHPDKNHHPRAEEAFKVLRAAWDIVSNPERRKEYE------MKRMAENELSRSVN 519
Cdd:PRK14283   8 YEVLGVDRNADKKEIKKAYRKLARKYHPDVSEEEGAEEKFKEISEAYAVLSDDEKRQRYDqfghagMDGFSQEDIFNNIN 87
PRK14276 PRK14276
chaperone protein DnaJ; Provisional
446-505 1.25e-12

chaperone protein DnaJ; Provisional


Pssm-ID: 237653 [Multi-domain]  Cd Length: 380  Bit Score: 70.12  E-value: 1.25e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 161760675 446 FHVLGVEATASDIELKKAYRQLAVMVHPDKNHHPRAEEAFKVLRAAWDIVSNPERRKEYE 505
Cdd:PRK14276   7 YDRLGVSKDASQDEIKKAYRKLSKKYHPDINKEPGAEEKYKEVQEAYETLSDPQKRAAYD 66
PRK14297 PRK14297
molecular chaperone DnaJ;
446-505 3.07e-12

molecular chaperone DnaJ;


Pssm-ID: 184611 [Multi-domain]  Cd Length: 380  Bit Score: 68.66  E-value: 3.07e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 161760675 446 FHVLGVEATASDIELKKAYRQLAVMVHPDKNH-HPRAEEAFKVLRAAWDIVSNPERRKEYE 505
Cdd:PRK14297   7 YEVLGLEKGASDDEIKKAFRKLAIKYHPDKNKgNKEAEEKFKEINEAYQVLSDPQKKAQYD 67
PRK14278 PRK14278
chaperone protein DnaJ; Provisional
448-506 4.62e-12

chaperone protein DnaJ; Provisional


Pssm-ID: 237654 [Multi-domain]  Cd Length: 378  Bit Score: 68.16  E-value: 4.62e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 161760675 448 VLGVEATASDIELKKAYRQLAVMVHPDKNHHPRAEEAFKVLRAAWDIVSNPERRKEYEM 506
Cdd:PRK14278   8 LLGVSRNASDAEIKRAYRKLARELHPDVNPDEEAQEKFKEISVAYEVLSDPEKRRIVDL 66
terminal_TopJ NF037946
terminal organelle assembly protein TopJ;
446-505 1.45e-11

terminal organelle assembly protein TopJ;


Pssm-ID: 468284 [Multi-domain]  Cd Length: 440  Bit Score: 67.15  E-value: 1.45e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 161760675 446 FHVLGVEATASDIELKKAYRQLAVMVHPDKNHHPRAEEAFKVLRAAWDIVSNPERRKEYE 505
Cdd:NF037946   8 YEVLGVDRDADDQEIKKAFRKLAKKYHPDRNKAPDAAEIFAEINEAYEVLSNPEKRANYD 67
PRK14277 PRK14277
chaperone protein DnaJ; Provisional
446-505 1.51e-11

chaperone protein DnaJ; Provisional


Pssm-ID: 184599 [Multi-domain]  Cd Length: 386  Bit Score: 66.75  E-value: 1.51e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 161760675 446 FHVLGVEATASDIELKKAYRQLAVMVHPDKN-HHPRAEEAFKVLRAAWDIVSNPERRKEYE 505
Cdd:PRK14277   8 YEILGVDRNATEEEIKKAYRRLAKKYHPDLNpGDKEAEQKFKEINEAYEILSDPQKRAQYD 68
PRK14281 PRK14281
chaperone protein DnaJ; Provisional
446-505 1.69e-11

chaperone protein DnaJ; Provisional


Pssm-ID: 237657 [Multi-domain]  Cd Length: 397  Bit Score: 66.76  E-value: 1.69e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 161760675 446 FHVLGVEATASDIELKKAYRQLAVMVHPDKN-HHPRAEEAFKVLRAAWDIVSNPERRKEYE 505
Cdd:PRK14281   6 YEVLGVSRSADKDEIKKAYRKLALKYHPDKNpDNKEAEEHFKEVNEAYEVLSNDDKRRRYD 66
PRK14299 PRK14299
chaperone protein DnaJ; Provisional
446-505 2.98e-11

chaperone protein DnaJ; Provisional


Pssm-ID: 237667 [Multi-domain]  Cd Length: 291  Bit Score: 64.96  E-value: 2.98e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 161760675 446 FHVLGVEATASDIELKKAYRQLAVMVHPDKNHHPRAEEAFKVLRAAWDIVSNPERRKEYE 505
Cdd:PRK14299   7 YAILGVPKNASQDEIKKAFKKLARKYHPDVNKSPGAEEKFKEINEAYTVLSDPEKRRIYD 66
PRK14286 PRK14286
chaperone protein DnaJ; Provisional
446-505 4.97e-11

chaperone protein DnaJ; Provisional


Pssm-ID: 172774 [Multi-domain]  Cd Length: 372  Bit Score: 65.01  E-value: 4.97e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 161760675 446 FHVLGVEATASDIELKKAYRQLAVMVHPDKNH-HPRAEEAFKVLRAAWDIVSNPERRKEYE 505
Cdd:PRK14286   7 YDILGVSKSANDEEIKSAYRKLAIKYHPDKNKgNKESEEKFKEATEAYEILRDPKKRQAYD 67
PRK14287 PRK14287
chaperone protein DnaJ; Provisional
446-505 6.15e-11

chaperone protein DnaJ; Provisional


Pssm-ID: 237659 [Multi-domain]  Cd Length: 371  Bit Score: 64.65  E-value: 6.15e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 161760675 446 FHVLGVEATASDIELKKAYRQLAVMVHPDKNHHPRAEEAFKVLRAAWDIVSNPERRKEYE 505
Cdd:PRK14287   7 YEVLGVDRNASVDEVKKAYRKLARKYHPDVNKAPDAEDKFKEVKEAYDTLSDPQKKAHYD 66
PRK14301 PRK14301
chaperone protein DnaJ; Provisional
446-505 8.78e-11

chaperone protein DnaJ; Provisional


Pssm-ID: 237668 [Multi-domain]  Cd Length: 373  Bit Score: 64.38  E-value: 8.78e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 161760675 446 FHVLGVEATASDIELKKAYRQLAVMVHPDKN-HHPRAEEAFKVLRAAWDIVSNPERRKEYE 505
Cdd:PRK14301   7 YEVLGVSRDASEDEIKKAYRKLALQYHPDRNpDNPEAEQKFKEAAEAYEVLRDAEKRARYD 67
PRK10266 PRK10266
curved DNA-binding protein;
446-513 1.37e-10

curved DNA-binding protein;


Pssm-ID: 182347 [Multi-domain]  Cd Length: 306  Bit Score: 62.92  E-value: 1.37e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 161760675 446 FHVLGVEATASDIELKKAYRQLAVMVHPDKNHHPRAEEAFKVLRAAWDIVSNPERRKEYEMKRMAENE 513
Cdd:PRK10266   7 YAIMGVKPTDDLKTIKTAYRRLARKYHPDVSKEPDAEARFKEVAEAWEVLSDEQRRAEYDQLWQHRND 74
PRK14292 PRK14292
chaperone protein DnaJ; Provisional
446-505 1.75e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 237662 [Multi-domain]  Cd Length: 371  Bit Score: 63.37  E-value: 1.75e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 161760675 446 FHVLGVEATASDIELKKAYRQLAVMVHPDKNHHPRAEEAFKVLRAAWDIVSNPERRKEYE 505
Cdd:PRK14292   5 YELLGVSRTASADEIKSAYRKLALKYHPDRNKEKGAAEKFAQINEAYAVLSDAEKRAHYD 64
PRK14280 PRK14280
molecular chaperone DnaJ;
446-505 2.26e-10

molecular chaperone DnaJ;


Pssm-ID: 237656 [Multi-domain]  Cd Length: 376  Bit Score: 62.82  E-value: 2.26e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 161760675 446 FHVLGVEATASDIELKKAYRQLAVMVHPDKNHHPRAEEAFKVLRAAWDIVSNPERRKEYE 505
Cdd:PRK14280   7 YEVLGVSKSASKDEIKKAYRKLSKKYHPDINKEEGADEKFKEISEAYEVLSDDQKRAQYD 66
PRK14293 PRK14293
molecular chaperone DnaJ;
446-505 2.85e-10

molecular chaperone DnaJ;


Pssm-ID: 237663 [Multi-domain]  Cd Length: 374  Bit Score: 62.70  E-value: 2.85e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 161760675 446 FHVLGVEATASDIELKKAYRQLAVMVHPDKNHHPRAEEAFKVLRAAWDIVSNPERRKEYE 505
Cdd:PRK14293   6 YEILGVSRDADKDELKRAYRRLARKYHPDVNKEPGAEDRFKEINRAYEVLSDPETRARYD 65
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
444-502 3.73e-10

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


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 56.34  E-value: 3.73e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 161760675 444 NPFHVLGVEATASDIELKKAYRQLAVMVHPDKNHHPRAEEAFKV-------LRAAWDIVSNPERRK 502
Cdd:COG1076    5 DAFELLGLPPDADDAELKRAYRKLQREHHPDRLAAGLPEEEQRLalqkaaaINEAYETLKDPRGID 70
PRK14290 PRK14290
chaperone protein DnaJ; Provisional
446-505 4.42e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 172778 [Multi-domain]  Cd Length: 365  Bit Score: 61.87  E-value: 4.42e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 161760675 446 FHVLGVEATASDIELKKAYRQLAVMVHPDKN--HHPRAEEAFKVLRAAWDIVSNPERRKEYE 505
Cdd:PRK14290   6 YKILGVDRNASQEDIKKAFRELAKKWHPDLHpgNKAEAEEKFKEISEAYEVLSDPQKRRQYD 67
PRK14284 PRK14284
chaperone protein DnaJ; Provisional
446-537 4.44e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 237658 [Multi-domain]  Cd Length: 391  Bit Score: 62.17  E-value: 4.44e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161760675 446 FHVLGVEATASDIELKKAYRQLAVMVHPDKNH-HPRAEEAFKVLRAAWDIVSNPERRKEYEmkRMAENELSRSVNEFLSK 524
Cdd:PRK14284   4 YTILGVSKTASPEEIKKAYRKLAVKYHPDKNPgDAEAEKRFKEVSEAYEVLSDAQKRESYD--RYGKDGPFAGAGGFGGA 81
                         90
                 ....*....|...
gi 161760675 525 LQDDLKEAMNTMM 537
Cdd:PRK14284  82 GMGNMEDALRTFM 94
PRK14282 PRK14282
chaperone protein DnaJ; Provisional
446-505 1.62e-09

chaperone protein DnaJ; Provisional


Pssm-ID: 184603 [Multi-domain]  Cd Length: 369  Bit Score: 60.19  E-value: 1.62e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 161760675 446 FHVLGVEATASDIELKKAYRQLAVMVHPDKNHHPR--AEEAFKVLRAAWDIVSNPERRKEYE 505
Cdd:PRK14282   7 YEILGVSRNATQEEIKRAYKRLVKEWHPDRHPENRkeAEQKFKEIQEAYEVLSDPQKRAMYD 68
PRK14296 PRK14296
chaperone protein DnaJ; Provisional
446-505 1.63e-09

chaperone protein DnaJ; Provisional


Pssm-ID: 237666 [Multi-domain]  Cd Length: 372  Bit Score: 60.35  E-value: 1.63e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 161760675 446 FHVLGVEATASDIELKKAYRQLAVMVHPDKNHHPRAEEAFKVLRAAWDIVSNPERRKEYE 505
Cdd:PRK14296   7 YEVLGVSKTASEQEIRQAYRKLAKQYHPDLNKSPDAHDKMVEINEAADVLLDKDKRKQYD 66
PRK14294 PRK14294
chaperone protein DnaJ; Provisional
446-505 2.01e-09

chaperone protein DnaJ; Provisional


Pssm-ID: 237664 [Multi-domain]  Cd Length: 366  Bit Score: 59.78  E-value: 2.01e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 161760675 446 FHVLGVEATASDIELKKAYRQLAVMVHPDKNHHPR-AEEAFKVLRAAWDIVSNPERRKEYE 505
Cdd:PRK14294   7 YEILGVTRDASEEEIKKSYRKLAMKYHPDRNPGDKeAEELFKEAAEAYEVLSDPKKRGIYD 67
PTZ00037 PTZ00037
DnaJ_C chaperone protein; Provisional
446-505 3.28e-09

DnaJ_C chaperone protein; Provisional


Pssm-ID: 240236 [Multi-domain]  Cd Length: 421  Bit Score: 59.45  E-value: 3.28e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 161760675 446 FHVLGVEATASDIELKKAYRQLAVMVHPDKNHHPraeEAFKVLRAAWDIVSNPERRKEYE 505
Cdd:PTZ00037  31 YEVLNLSKDCTTSEIKKAYRKLAIKHHPDKGGDP---EKFKEISRAYEVLSDPEKRKIYD 87
PRK14300 PRK14300
chaperone protein DnaJ; Provisional
446-505 3.51e-09

chaperone protein DnaJ; Provisional


Pssm-ID: 172788 [Multi-domain]  Cd Length: 372  Bit Score: 59.26  E-value: 3.51e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 161760675 446 FHVLGVEATASDIELKKAYRQLAVMVHPDKNHHPRAEEAFKVLRAAWDIVSNPERRKEYE 505
Cdd:PRK14300   6 YQILGVSKTASQADLKKAYLKLAKQYHPDTTDAKDAEKKFKEINAAYDVLKDEQKRAAYD 65
PRK14285 PRK14285
chaperone protein DnaJ; Provisional
446-505 2.49e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 172773 [Multi-domain]  Cd Length: 365  Bit Score: 53.46  E-value: 2.49e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 161760675 446 FHVLGVEATASDIELKKAYRQLAVMVHPDKNH-HPRAEEAFKVLRAAWDIVSNPERRKEYE 505
Cdd:PRK14285   6 YEILGLSKGASKDEIKKAYRKIAIKYHPDKNKgNKEAESIFKEATEAYEVLIDDNKRAQYD 66
PRK14288 PRK14288
molecular chaperone DnaJ;
442-527 6.26e-06

molecular chaperone DnaJ;


Pssm-ID: 172776 [Multi-domain]  Cd Length: 369  Bit Score: 48.92  E-value: 6.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161760675 442 ELNPFHVLGVEATASDIELKKAYRQLAVMVHPDKNHHPR-AEEAFKVLRAAWDIVSNPERRKEYE-MKRMAENELSRSVN 519
Cdd:PRK14288   2 ELSYYEILEVEKHSNQETIKKSYRKLALKYHPDRNAGDKeAEEKFKLINEAYGVLSDEKKRALYDrYGKKGLNQAGASQS 81

                 ....*...
gi 161760675 520 EFLSKLQD 527
Cdd:PRK14288  82 DFSDFFED 89
djlA PRK09430
co-chaperone DjlA;
446-475 1.66e-04

co-chaperone DjlA;


Pssm-ID: 236512 [Multi-domain]  Cd Length: 267  Bit Score: 44.03  E-value: 1.66e-04
                         10        20        30
                 ....*....|....*....|....*....|
gi 161760675 446 FHVLGVEATASDIELKKAYRQLAVMVHPDK 475
Cdd:PRK09430 203 YKVLGVSESDDDQEIKRAYRKLMSEHHPDK 232
 
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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